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6Y9B

Cryo-EM structure of trimeric human STEAP1 bound to three Fab120.545 fragments

Functional Information from GO Data
ChainGOidnamespacecontents
A0005515molecular_functionprotein binding
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
B0005515molecular_functionprotein binding
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
C0005515molecular_functionprotein binding
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 PDB Data
site_idAC1
Number of Residues12
Detailsbinding site for residue HEM C 401
ChainResidue
CLYS116
CPHE272
CTHR290
CPHE291
CPRO119
CSER122
CHIS175
CALA176
CSER179
CGLY223
CLEU227
CHIS268

site_idAC2
Number of Residues10
Detailsbinding site for residue XP4 C 402
ChainResidue
ALEU232
AVAL235
CPHE68
CGLN70
CTRP71
CPHE170
CVAL173
CALA234
CSER237
CPRO239

site_idAC3
Number of Residues12
Detailsbinding site for residue HEM A 401
ChainResidue
ALYS116
APRO119
ASER122
AHIS175
AALA176
ASER179
AGLY223
ALEU227
AHIS268
APHE272
ATHR290
APHE291

site_idAC4
Number of Residues10
Detailsbinding site for residue XP4 A 402
ChainResidue
APHE68
AGLN70
ATRP71
APHE170
AVAL173
AALA234
ASER237
APRO239
BLEU232
BVAL235

site_idAC5
Number of Residues12
Detailsbinding site for residue HEM B 401
ChainResidue
BLYS116
BPRO119
BSER122
BHIS175
BALA176
BSER179
BGLY223
BLEU227
BHIS268
BPHE272
BTHR290
BPHE291

site_idAC6
Number of Residues10
Detailsbinding site for residue XP4 B 402
ChainResidue
BPHE68
BGLN70
BTRP71
BPHE170
BVAL173
BALA234
BSER237
BPRO239
CALA231
CVAL235

Functional Information from PROSITE/UniProt
site_idPS00290
Number of Residues7
DetailsIG_MHC Immunoglobulins and major histocompatibility complex proteins signature. YACEVTH
ChainResidueDetails
LTYR198-HIS204
HTYR205-HIS211

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

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

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

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PDB entries from 2024-08-14

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