Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

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
DetailsTransmembrane: {"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues12
DetailsBinding site: {"evidences":[{"source":"UniProtKB","id":"Q687X5","evidenceCode":"ECO:0000250"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"description":"axial binding residue","evidences":[{"source":"PubMed","id":"32409586","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"6Y9B","evidenceCode":"ECO:0007744"}]}
ChainResidueDetails

239803

PDB entries from 2025-08-06

PDB statisticsPDBj update infoContact PDBjnumon