Hemopexin (HPX) is a secreted plasma glycoprotein (~60 kDa) that binds free heme with the highest affinity of any known protein (Kd < 10^-13 M). It serves as the primary scavenger of free heme released from hemoproteins during hemolysis, hemorrhage, and other pathological states. HPX transports heme to the liver for degradation and iron recovery via receptor-mediated endocytosis through LRP1/CD91 (Kd ~4 nM for LRP1). Recent cell-biology work shows HPX uptake is not exclusively LRP1-dependent: HPX co-traffics with transferrin receptor 1 (TfR1) in Rab5-positive early endosomes, and heme–HPX endocytosis still occurs in LRP1-/- cells, implying additional receptor routes. Heme delivery via HPX initiates a cytoprotective program including HMOX1/HO-1 induction and ferritin storage. This prevents heme-mediated oxidative damage, inflammatory activation, and iron loss. HPX exhibits 1:1 heme binding at low heme concentrations and ≥2:1 (heme:HPX) at higher loads, circulating in plasma at ~0.5–1.5 mg/mL, with HPX also present in cerebrospinal fluid and lymph. The protein is synthesized primarily in hepatocytes and is an acute-phase protein induced by IL-6 and other pro-inflammatory cytokines during infection and inflammation.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005615 extracellular space | IBA GO_REF:0000033 | ACCEPT | Summary: HPX is a secreted plasma glycoprotein that functions in the extracellular space. UniProt annotates it as "Secreted" and notes it is "Expressed by the liver and secreted in plasma." The deep research confirms HPX "circulates as a plasma protein" with plasma concentrations of 0.5-1.5 mg/mL. This IBA annotation is phylogenetically supported and represents a core localization. Reason: Extracellular space is the primary site of HPX function where it scavenges free heme from plasma. This is unambiguously supported by UniProt subcellular location annotation and extensive literature. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md Hemopexin circulates in plasma at concentrations of 0.5-1.5 mg/mL and functions as a critical component of the body's defense system against heme toxicity by scavenging free heme released from hemoproteins during hemolysis, hemorrhage, and other pathological states |
| GO:0042168 heme metabolic process | IBA GO_REF:0000033 | ACCEPT | Summary: HPX is directly involved in heme metabolism by binding and transporting heme for catabolism. The deep research states that HPX delivers heme to hepatocytes where "the heme is rapidly catabolized by heme oxygenase enzymes." This IBA annotation is phylogenetically supported. Reason: HPX plays a central role in heme metabolism by scavenging free heme and delivering it to the liver for degradation by heme oxygenase, followed by iron recycling. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md The heme detoxification process is primarily driven by hemopexin through CD91/LRP1-mediated endocytosis in the liver, leading to heme degradation, reutilization, and iron metabolism, with some hemopexin molecules being recycled back into the plasma PMID:41384245 In cultured cells, heme–HPX binding and heme delivery initiate a "cytoprotective" program of events (Montecinos et al., 2019), including the induction of the heme degrading enzyme heme oxygenase (HMOX1). The iron from heme induces ferritin for iron storage |
| GO:0005576 extracellular region | IEA GO_REF:0000044 | ACCEPT | Summary: HPX is a secreted protein that functions in the extracellular region. This IEA annotation from UniProtKB subcellular location mapping is correct but less specific than extracellular space (GO:0005615). Reason: Correct annotation - HPX is secreted into plasma. While extracellular space is more specific, extracellular region is also accurate. Supporting Evidence: file:human/HPX/HPX-uniprot.txt SUBCELLULAR LOCATION: Secreted. |
| GO:0006879 intracellular iron ion homeostasis | IEA GO_REF:0000002 | ACCEPT | Summary: HPX contributes to iron homeostasis by recovering iron from heme during catabolism. The deep research explains that "the iron released from heme catabolism is either bound to ferritin for storage or exported from cells to hematopoietic tissues via the iron-transporter ferroportin." Reason: HPX-mediated heme scavenging is essential for iron conservation and recycling. The iron from HPX-delivered heme is recovered and redistributed for erythropoiesis. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md Hemopexin preserves the body's iron through this efficient recycling pathway, ensuring that iron from catabolized hemoproteins is recovered and made available for new hemoglobin synthesis rather than being lost through excretion or deposition in tissues |
| GO:0015232 heme transmembrane transporter activity | IEA GO_REF:0000002 | REMOVE | Summary: This annotation is INCORRECT. HPX is NOT a transmembrane transporter. It is a soluble plasma protein that binds heme in the extracellular space and delivers it to cells via receptor-mediated endocytosis through LRP1/CD91. HPX does not span the membrane or function as a transmembrane channel or carrier. Reason: HPX is a soluble heme-binding plasma protein, not a transmembrane transporter. The actual transmembrane transport of heme occurs through other proteins like FLVCR1. HPX functions by binding heme extracellularly and being endocytosed with its cargo. This IEA annotation from InterPro mapping is erroneous. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md Hemopexin enters cells through receptor-mediated endocytosis following binding to the LRP1/CD91 receptor on the cell surface. Following ligand binding, hemopexin-heme complexes are internalized via clathrin-mediated endocytosis file:human/HPX/HPX-uniprot.txt SUBCELLULAR LOCATION: Secreted. |
| GO:0015886 heme transport | IEA GO_REF:0000002 | ACCEPT | Summary: HPX is the primary heme transport protein in plasma. It binds free heme with the highest affinity of any known protein and transports it to the liver for degradation. The deep research confirms this core function. Reason: Heme transport is a core function of HPX. It scavenges free heme from plasma and transports it to hepatocytes and macrophages via LRP1-mediated endocytosis. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md The primary and most extensively characterized function of hemopexin is the binding and scavenging of free heme with affinity exceeding all other known proteins in the human proteome file:human/HPX/HPX-uniprot.txt Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation. PMID:38022615 HPX plays a multifaceted role by sequestering free heme released from haptoglobin, participating in heme transport, and preventing peroxidation damage by induction of heme oxygenase 1 (HO-1) and metalloproteinase 1 genes |
| GO:0046872 metal ion binding | IEA GO_REF:0000043 | KEEP AS NON CORE | Summary: HPX does bind metal ions - specifically the iron within the heme porphyrin ring. However, this annotation is too generic and does not capture the specific function of HPX, which is heme binding rather than general metal ion binding. Reason: While technically correct (HPX binds iron as part of heme), this term is too general to be informative about HPX's specific function. Heme binding (GO:0020037) is the appropriate specific term for HPX's molecular function. Supporting Evidence: file:human/HPX/HPX-uniprot.txt Iron; Metal-binding |
| GO:0005515 protein binding | IPI PMID:28514442 Architecture of the human interactome defines protein commun... | REMOVE | Summary: This annotation comes from a large-scale interactome study. Protein binding is too generic to be informative about HPX function. Reason: Generic protein binding annotation does not inform about HPX's specific function. HPX does interact with LRP1/CD91 and FLVCR1, but these should be annotated with more specific terms if needed. Protein binding without context is uninformative. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md [large-scale interactome study] Architecture of the human interactome defines protein communities and disease networks PMID:28514442 Architecture of the human interactome defines protein communities and disease networks. |
| GO:0005515 protein binding | IPI PMID:33961781 Dual proteome-scale networks reveal cell-specific remodeling... | REMOVE | Summary: This is a duplicate protein binding annotation from another interactome study. Too generic to be informative. Reason: Generic protein binding annotation does not inform about HPX's specific function. Large-scale interactome studies generate many non-specific annotations. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md [large-scale interactome study] Dual proteome-scale networks reveal cell-specific remodeling of the human interactome PMID:33961781 2021 May 6. Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. |
| GO:0002639 positive regulation of immunoglobulin production | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This annotation is transferred from ortholog data via Ensembl Compara. There is limited direct evidence for HPX regulating immunoglobulin production in humans. The deep research mentions HPX has immunomodulatory effects but focuses on cytokine regulation, not immunoglobulin production. Reason: While HPX has immunomodulatory properties, direct evidence for regulating immunoglobulin production is limited. This appears to be an over-annotation from ortholog transfer that may reflect indirect or pleiotropic effects rather than a core function. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md Hemopexin downregulates lipopolysaccharide (LPS)-induced production of the inflammatory cytokines tumor necrosis factor-alpha (TNF-alpha) and interleukin-6 (IL-6) in mouse bone marrow-derived macrophages |
| GO:0002925 positive regulation of humoral immune response mediated by circulating immunoglobulin | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Similar to the immunoglobulin production annotation, this is transferred from ortholog data and lacks direct experimental support for HPX in humans. Reason: This appears to be an indirect or pleiotropic effect transferred from ortholog data. Not a core function of HPX. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md [ortholog transfer annotation] Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara |
| GO:0020027 hemoglobin metabolic process | IEA GO_REF:0000107 | ACCEPT | Summary: HPX scavenges heme released from hemoglobin during hemolysis, indirectly contributing to hemoglobin metabolism. The deep research describes how HPX receives heme transferred from hemoglobin in a sequential process. Reason: HPX is involved in processing hemoglobin-derived heme. It receives heme transferred from oxidized hemoglobin and transports it for catabolism. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md Studies highlight that the heme moiety can be transferred from hemoglobin to hemopexin, and this transfer preferentially occurs when heme is oxidized to its ferric form. The process appears to proceed in a four-stage process in which hemopexin successively transfers all four heme groups from the hemoglobin tetramer |
| GO:0042168 heme metabolic process | IEA GO_REF:0000107 | ACCEPT | Summary: Duplicate of the IBA annotation above. HPX is central to heme metabolism. Reason: Core function of HPX - heme scavenging and delivery for catabolism. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md The main function of hemopexin is scavenging the heme released or lost by the turnover of heme proteins such as hemoglobin and thus protecting the body from the oxidative damage that free heme can cause |
| GO:0051246 regulation of protein metabolic process | IEA GO_REF:0000107 | KEEP AS NON CORE | Summary: HPX does affect gene expression and protein metabolism through heme signaling - particularly inducing heme oxygenase-1 expression. However, this term is very broad and not specific to HPX's primary function. Reason: While HPX does affect protein metabolism through inducing HO-1 and other genes, this is a secondary/downstream effect of its heme delivery function, not a core function. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md Uptake of hemopexin-heme complex induced LRP/CD91-dependent heme-oxygenase 1 (HO-1) mRNA transcription in cultured monocytes |
| GO:0060332 positive regulation of response to type II interferon | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: This annotation is transferred from ortholog data. HPX does have immunomodulatory functions, but direct evidence for regulating type II interferon response specifically is limited. Reason: This appears to be a pleiotropic/indirect effect. Not a core function of HPX. The primary immunomodulatory effects of HPX are through heme sequestration and anti-inflammatory cytokine modulation. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md [ortholog transfer annotation] Beyond simple heme scavenging, hemopexin plays complex and multifaceted roles in immune regulation |
| GO:0060335 positive regulation of type II interferon-mediated signaling pathway | IEA GO_REF:0000107 | MARK AS OVER ANNOTATED | Summary: Same as above - transferred annotation with limited direct evidence for HPX-specific regulation of interferon signaling. Reason: Pleiotropic/indirect effect, not a core function of HPX. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md [ortholog transfer annotation] Beyond simple heme scavenging, hemopexin plays complex and multifaceted roles in immune regulation |
| GO:0031012 extracellular matrix | HDA PMID:28675934 Characterization of the Extracellular Matrix of Normal and D... | KEEP AS NON CORE | Summary: This is from a proteomics study characterizing extracellular matrix. HPX may be detected in ECM preparations as a contaminating plasma protein, but it is not a structural ECM component. Reason: HPX is a soluble plasma protein, not a structural ECM component. Detection in ECM proteomics likely reflects plasma contamination or transient association. Not a core localization. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md [proteomics study] Hemopexin circulates as a plasma protein but functions in multiple cellular and tissue compartments PMID:28675934 Characterization of the Extracellular Matrix of Normal and Diseased Tissues Using Proteomics. |
| GO:0070062 extracellular exosome | HDA PMID:23533145 In-depth proteomic analyses of exosomes isolated from expres... | KEEP AS NON CORE | Summary: HPX has been detected in exosomes by proteomics. This represents a secondary localization rather than primary function site. Reason: Proteomics detection in exosomes is valid but represents minor localization compared to plasma. Not a core localization. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md [proteomics study] Hemopexin circulates in plasma at concentrations of 0.5-1.5 mg/mL PMID:23533145 2013 Apr 23. In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine. |
| GO:0005615 extracellular space | HDA PMID:16502470 Human colostrum: identification of minor proteins in the aqu... | ACCEPT | Summary: Proteomics detection of HPX in human colostrum confirms its presence in extracellular fluids. This supports the core localization. Reason: Confirms core localization in extracellular space (plasma/body fluids). Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md Hemopexin circulates in plasma at concentrations of 0.5-1.5 mg/mL PMID:16502470 Human colostrum: identification of minor proteins in the aqueous phase by proteomics. |
| GO:0072562 blood microparticle | HDA PMID:22516433 Proteomic analysis of microvesicles from plasma of healthy d... | KEEP AS NON CORE | Summary: HPX detected in blood microparticles by proteomics. This represents a secondary localization. Reason: Detection in blood microparticles is valid but represents minor localization. HPX's primary function is as soluble plasma protein. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md [proteomics study] Hemopexin circulates in plasma at concentrations of 0.5-1.5 mg/mL PMID:22516433 Epub 2012 Apr 10. Proteomic analysis of microvesicles from plasma of healthy donors reveals high individual variability. |
| GO:0070062 extracellular exosome | HDA PMID:19056867 Large-scale proteomics and phosphoproteomics of urinary exos... | KEEP AS NON CORE | Summary: Duplicate exosome annotation from different proteomics study. Reason: Secondary localization, not core function site. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md [proteomics study] Hemopexin circulates in plasma at concentrations of 0.5-1.5 mg/mL PMID:19056867 2008 Dec 3. Large-scale proteomics and phosphoproteomics of urinary exosomes. |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2168884 | ACCEPT | Summary: Reactome pathway annotation for heme transfer from methemoglobin to HPX. Confirms extracellular localization where this transfer occurs. Reason: Core localization supported by pathway annotation. Supporting Evidence: Reactome:R-HSA-2168884 When haptoglobin capacity to buffer hemoglobin is overwhelmed, hemoglobin undergoes a rapid conversion to methemoglobin. Ferriheme is transferred directly from methemoglobin to hemopexin |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2168886 | ACCEPT | Summary: Reactome annotation for HPX binding hemes. Core function occurs in extracellular region. Reason: Core localization for heme binding function. Supporting Evidence: Reactome:R-HSA-2168886 Hemopexin binds either ferriheme b or ferroheme b, however the stability of the complex containing ferriheme b is greater than the stability of the complex containing ferroheme b |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2168887 | ACCEPT | Summary: Reactome annotation for heme transfer from albumin to HPX. Reason: Core localization for heme scavenging function. Supporting Evidence: Reactome:R-HSA-2168887 Despite the lower affinity of ferriheme for albumin than for hemopexin, ferriheme initially associates with albumin, presumably because the molar concentration of albumin in plasma is considerably greater than that of hemopexin. Ferriheme is transferred directly from serum albumin to hemopexin |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2168897 | ACCEPT | Summary: Reactome annotation for LRP1 binding HPX:heme complex at cell surface. Reason: Core localization for receptor binding function. Supporting Evidence: Reactome:R-HSA-2168897 Once formed in the plasma, the hemopexin:heme complex is rapidly cleared from circulation and it is taken up by the liver PMID:41384245 shown by surface plasmon resonance to be a high-affinity HPX-binding protein, Kd 4 nM (Hvidberg et al., 2005) |
| GO:0005576 extracellular region | TAS Reactome:R-HSA-2230983 | ACCEPT | Summary: Reactome annotation for HPX:heme endocytosis. HPX transitions from extracellular to endocytic vesicle. Reason: Core localization prior to endocytosis. Supporting Evidence: Reactome:R-HSA-2230983 The LRP1:hemopexin:heme complex is endocytosed and the complex is dissociated in lysosomes, leading to heme uptake |
| GO:0071682 endocytic vesicle lumen | TAS Reactome:R-HSA-2230983 | ACCEPT | Summary: After binding LRP1 and being endocytosed, HPX:heme complex is transported through endocytic vesicles. This is part of the heme delivery mechanism. Reason: Valid localization during the heme delivery process - HPX is internalized via clathrin-mediated endocytosis. Supporting Evidence: Reactome:R-HSA-2230983 The LRP1:hemopexin:heme complex is endocytosed and the complex is dissociated in lysosomes, leading to heme uptake. Heme is then degraded by heme oxygenases |
| GO:0005615 extracellular space | IDA PMID:19433579 Hemoglobin and its scavenger protein haptoglobin associate w... | ACCEPT | Summary: Direct experimental evidence for HPX in extracellular space from a study on HPX association with HDL and inflammatory properties. Reason: Core localization supported by direct assay. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md Hemopexin and haptoglobin associate with high-density lipoprotein (HDL) and influence the inflammatory properties of HDL PMID:19433579 2009 May 11. Hemoglobin and its scavenger protein haptoglobin associate with apoA-1-containing particles and influence the inflammatory properties and function of high density lipoprotein. |
| GO:0005515 protein binding | IPI PMID:20610401 Kinetics and specificity of feline leukemia virus subgroup C... | REMOVE | Summary: This annotation is from a study on HPX interaction with FLVCR1 (feline leukemia virus subgroup C receptor). While this specific interaction is documented in UniProt ("Interacts with FLVCR1"), the generic protein binding term is uninformative. Reason: While HPX-FLVCR1 interaction is real and documented, the generic protein binding term does not capture this specific interaction. A more specific annotation would be preferable. Supporting Evidence: file:human/HPX/HPX-uniprot.txt Interacts with FLVCR1 PMID:20610401 2010 Jul 7. Kinetics and specificity of feline leukemia virus subgroup C receptor (FLVCR) export function and its dependence on hemopexin. |
| GO:0005576 extracellular region | NAS PMID:14718574 The human plasma proteome: a nonredundant list developed by ... | ACCEPT | Summary: HPX identified in human plasma proteome study confirming extracellular localization. Reason: Core localization supported by plasma proteomics. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md Hemopexin circulates in plasma at concentrations of 0.5-1.5 mg/mL PMID:14718574 Epub 2004 Jan 12. The human plasma proteome: a nonredundant list developed by combination of four separate sources. |
| GO:0005615 extracellular space | TAS PMID:3855550 Complete amino acid sequence of human hemopexin, the heme-bi... | ACCEPT | Summary: The original paper describing the complete amino acid sequence of human hemopexin confirms it is a serum protein. Reason: Core localization from foundational characterization study. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md The primary structure of human hemopexin has been deduced through sequence analysis of peptides obtained from chemical and enzymatic digests PMID:3855550 Complete amino acid sequence of human hemopexin, the heme-binding protein of serum. |
| GO:0006879 intracellular iron ion homeostasis | TAS PMID:3855550 Complete amino acid sequence of human hemopexin, the heme-bi... | ACCEPT | Summary: The foundational paper establishes HPX's role in iron recovery. By transporting heme to the liver for breakdown, HPX enables iron recycling. Reason: Core function - HPX-mediated heme transport is essential for iron conservation and homeostasis. Supporting Evidence: file:human/HPX/HPX-uniprot.txt Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation. PMID:3855550 Complete amino acid sequence of human hemopexin, the heme-binding protein of serum. |
| GO:0015232 heme transmembrane transporter activity | TAS PMID:3855550 Complete amino acid sequence of human hemopexin, the heme-bi... | REMOVE | Summary: This annotation is INCORRECT. The cited paper describes HPX as a soluble heme-binding serum protein, NOT a transmembrane transporter. HPX does not span the membrane. Reason: Erroneous annotation. HPX is a soluble plasma protein that binds heme extracellularly and is endocytosed with its cargo via LRP1. It is not a transmembrane transporter. The original reference does not support this annotation. Supporting Evidence: file:human/HPX/HPX-uniprot.txt SUBCELLULAR LOCATION: Secreted. PMID:3855550 Complete amino acid sequence of human hemopexin, the heme-binding protein of serum. |
| GO:0015886 heme transport | TAS PMID:3855550 Complete amino acid sequence of human hemopexin, the heme-bi... | ACCEPT | Summary: The foundational paper establishes HPX as a heme-binding protein that transports heme to the liver. Reason: Core function - HPX is the primary heme transport protein in plasma. Supporting Evidence: file:human/HPX/HPX-uniprot.txt Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation. PMID:3855550 Complete amino acid sequence of human hemopexin, the heme-binding protein of serum. |
| GO:0020037 heme binding | IDA PMID:3855550 Complete amino acid sequence of human hemopexin, the heme-bi... | NEW | Summary: Heme binding is the primary molecular function of HPX. It binds heme with the highest affinity of any known protein (Kd < 10^-13 M). This core function is missing from the existing GO annotations and should be added. Reason: Core molecular function of HPX. The protein binds heme via histidine residues (H79, H150, H236, H293) in the hemopexin domains. Structural studies have characterized the heme-binding site in detail. Supporting Evidence: file:human/HPX/HPX-deep-research-perplexity.md Hemopexin binds heme with the highest affinity of any known protein, with a dissociation constant (Kd) estimated at less than 10^-13 M, representing binding affinity that is extraordinary even among high-affinity protein-ligand interactions file:human/HPX/HPX-uniprot.txt Binds heme and transports it to the liver for breakdown and iron recovery, after which the free hemopexin returns to the circulation. PMID:3855550 Complete amino acid sequence of human hemopexin, the heme-binding protein of serum. PMID:38022615 It is a plasma glycoprotein composed of a single 60-kDa peptide chain, known for its exceptional binding affinity to heme. HPX exhibits a 1:1 binding ratio with heme at low concentrations and at least a 2:1 ratio (heme: hemopexin) at higher heme concentrations. file:human/HPX/HPX-deep-research-falcon.md Hemopexin is described as a **plasma glycoprotein (~60 kDa)** and the **highest-affinity heme-binding protein in plasma**, functioning as a systemic heme scavenger during hemolysis. |
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Q: Should the heme transmembrane transporter activity annotations be corrected in the source databases?
Experiment: Quantitative binding studies comparing HPX heme-binding affinity with other heme-binding proteins.
Experiment: Structural characterization of human HPX-heme complex (current crystal structure is from rabbit).
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