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1RQ1

Structure of Ero1p, Source of Disulfide Bonds for Oxidative Protein Folding in the Cell

Functional Information from GO Data
ChainGOidnamespacecontents
A0005783cellular_componentendoplasmic reticulum
A0015035molecular_functionprotein-disulfide reductase activity
A0016972molecular_functionthiol oxidase activity
A0034975biological_processprotein folding in endoplasmic reticulum
A0071949molecular_functionFAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE CD A 813
ChainResidue
AHIS237
AGLU241
AGLU408
AHOH829

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE CD A 814
ChainResidue
AHIS386
ALYS390

site_idAC3
Number of Residues3
DetailsBINDING SITE FOR RESIDUE NEN A 501
ChainResidue
AGLN205
ACYS208
ATYR420

site_idAC4
Number of Residues23
DetailsBINDING SITE FOR RESIDUE FAD A 634
ChainResidue
AASP108
AGLU186
AARG187
APHE188
ATHR189
AGLY190
ATYR191
AALA196
AILE199
ATRP200
ATYR204
ATYR224
ASER228
AHIS231
AALA232
AILE234
ALEU238
AARG260
AARG267
AMET347
ACYS355
AHOH820
AHOH871

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues1
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"15163408","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues1
DetailsActive site: {"evidences":[{"source":"PubMed","id":"15163408","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues6
DetailsBinding site: {"evidences":[{"source":"PubMed","id":"15163408","evidenceCode":"ECO:0000269"}]}
ChainResidueDetails

site_idSWS_FT_FI4
Number of Residues2
DetailsGlycosylation: {"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

247536

PDB entries from 2026-01-14

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