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8UCD

Cryo-EM structure of human STEAP1 in complex with AMG 509 Fab

Functional Information from GO Data
ChainGOidnamespacecontents
A0005768cellular_componentendosome
A0005886cellular_componentplasma membrane
A0005911cellular_componentcell-cell junction
A0010008cellular_componentendosome membrane
A0016020cellular_componentmembrane
A0020037molecular_functionheme binding
A0046872molecular_functionmetal ion binding
A0052851molecular_functionferric-chelate reductase (NADPH) activity
B0005768cellular_componentendosome
B0005886cellular_componentplasma membrane
B0005911cellular_componentcell-cell junction
B0010008cellular_componentendosome membrane
B0016020cellular_componentmembrane
B0020037molecular_functionheme binding
B0046872molecular_functionmetal ion binding
B0052851molecular_functionferric-chelate reductase (NADPH) activity
C0005768cellular_componentendosome
C0005886cellular_componentplasma membrane
C0005911cellular_componentcell-cell junction
C0010008cellular_componentendosome membrane
C0016020cellular_componentmembrane
C0020037molecular_functionheme binding
C0046872molecular_functionmetal ion binding
C0052851molecular_functionferric-chelate reductase (NADPH) activity
Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
LTYR312-HIS318

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues360
DetailsTRANSMEM: Helical => ECO:0000255
ChainResidueDetails
ATRP71-LEU91
BILE218-ILE238
BGLY258-ILE278
BPHE291-PRO311
CTRP71-LEU91
CPRO119-VAL139
CPHE164-MET184
CILE218-ILE238
CGLY258-ILE278
CPHE291-PRO311
APRO119-VAL139
APHE164-MET184
AILE218-ILE238
AGLY258-ILE278
APHE291-PRO311
BTRP71-LEU91
BPRO119-VAL139
BPHE164-MET184

site_idSWS_FT_FI2
Number of Residues12
DetailsBINDING: BINDING => ECO:0000250|UniProtKB:Q687X5
ChainResidueDetails
AGLN140
CARG161
CSER237
CGLN254
AARG161
ASER237
AGLN254
BGLN140
BARG161
BSER237
BGLN254
CGLN140

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: axial binding residue => ECO:0000305|PubMed:32409586, ECO:0007744|PDB:6Y9B
ChainResidueDetails
AHIS175
AHIS268
BHIS175
BHIS268
CHIS175
CHIS268

221051

PDB entries from 2024-06-12

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