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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
DetailsACT_SITE: Nucleophile => ECO:0000269|PubMed:15163408
ChainResidueDetails
ACYS352

site_idSWS_FT_FI2
Number of Residues1
DetailsACT_SITE: ACT_SITE => ECO:0000269|PubMed:15163408
ChainResidueDetails
ACYS355

site_idSWS_FT_FI3
Number of Residues6
DetailsBINDING: BINDING => ECO:0000269|PubMed:15163408
ChainResidueDetails
AARG187
ATHR189
ATRP200
ASER228
AHIS231
AARG260

site_idSWS_FT_FI4
Number of Residues2
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN130
AASN342

222624

PDB entries from 2024-07-17

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