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6HCY

human STEAP4 bound to NADP, FAD, heme and Fe(III)-NTA.

Functional Information from GO Data
ChainGOidnamespacecontents
A0000139cellular_componentGolgi membrane
A0005654cellular_componentnucleoplasm
A0005768cellular_componentendosome
A0005886cellular_componentplasma membrane
A0006811biological_processmonoatomic ion transport
A0006826biological_processiron ion transport
A0008823molecular_functioncupric reductase (NADH) activity
A0009055molecular_functionelectron transfer activity
A0010008cellular_componentendosome membrane
A0015677biological_processcopper ion import
A0016020cellular_componentmembrane
A0016491molecular_functionoxidoreductase activity
A0020037molecular_functionheme binding
A0031901cellular_componentearly endosome membrane
A0033212biological_processiron import into cell
A0045444biological_processfat cell differentiation
A0046872molecular_functionmetal ion binding
A0052851molecular_functionferric-chelate reductase (NADPH) activity
A0070062cellular_componentextracellular exosome
A0070207biological_processprotein homotrimerization
A0071949molecular_functionFAD binding
B0000139cellular_componentGolgi membrane
B0005654cellular_componentnucleoplasm
B0005768cellular_componentendosome
B0005886cellular_componentplasma membrane
B0006811biological_processmonoatomic ion transport
B0006826biological_processiron ion transport
B0008823molecular_functioncupric reductase (NADH) activity
B0009055molecular_functionelectron transfer activity
B0010008cellular_componentendosome membrane
B0015677biological_processcopper ion import
B0016020cellular_componentmembrane
B0016491molecular_functionoxidoreductase activity
B0020037molecular_functionheme binding
B0031901cellular_componentearly endosome membrane
B0033212biological_processiron import into cell
B0045444biological_processfat cell differentiation
B0046872molecular_functionmetal ion binding
B0052851molecular_functionferric-chelate reductase (NADPH) activity
B0070062cellular_componentextracellular exosome
B0070207biological_processprotein homotrimerization
B0071949molecular_functionFAD binding
C0000139cellular_componentGolgi membrane
C0005654cellular_componentnucleoplasm
C0005768cellular_componentendosome
C0005886cellular_componentplasma membrane
C0006811biological_processmonoatomic ion transport
C0006826biological_processiron ion transport
C0008823molecular_functioncupric reductase (NADH) activity
C0009055molecular_functionelectron transfer activity
C0010008cellular_componentendosome membrane
C0015677biological_processcopper ion import
C0016020cellular_componentmembrane
C0016491molecular_functionoxidoreductase activity
C0020037molecular_functionheme binding
C0031901cellular_componentearly endosome membrane
C0033212biological_processiron import into cell
C0045444biological_processfat cell differentiation
C0046872molecular_functionmetal ion binding
C0052851molecular_functionferric-chelate reductase (NADPH) activity
C0070062cellular_componentextracellular exosome
C0070207biological_processprotein homotrimerization
C0071949molecular_functionFAD binding
Functional Information from PROSITE/UniProt
site_idPS00024
Number of Residues15
DetailsHEMOPEXIN Hemopexin domain signature. LFpmWrf.PfYLSAVL
ChainResidueDetails
CLEU196-LEU210

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues366
DetailsTransmembrane: {"description":"Helical","evidences":[{"source":"PubMed","id":"30337524","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues444
DetailsDomain: {"description":"Ferric oxidoreductase","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues48
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"30337524","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6HCY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q4V8K1","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI5
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q658P3","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI6
Number of Residues6
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"30337524","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6HCY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

site_idSWS_FT_FI7
Number of Residues3
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"source":"PubMed","id":"19159218","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30337524","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"6HCY","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

243083

PDB entries from 2025-10-15

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