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3AHQ

hyperactive human Ero1

Functional Information from GO Data
ChainGOidnamespacecontents
A0005783cellular_componentendoplasmic reticulum
A0015035molecular_functionprotein-disulfide reductase activity
A0016491molecular_functionoxidoreductase activity
A0016972molecular_functionthiol oxidase activity
A0034975biological_processprotein folding in endoplasmic reticulum
A0071949molecular_functionFAD binding
Functional Information from PDB Data
site_idAC1
Number of Residues25
DetailsBINDING SITE FOR RESIDUE FAD A 1
ChainResidue
AARG187
ASER252
AHIS255
AALA256
AILE258
AASN259
ALEU262
ALYS276
ATRP277
AARG287
AARG300
ATYR188
AMET389
ACYS397
AHOH470
AHOH482
AHOH488
AHOH493
ATHR189
ATYR191
AALA196
ATRP197
ATRP200
ATYR204
ATYR248

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues7
DetailsBINDING: BINDING => ECO:0000269|PubMed:20834232, ECO:0007744|PDB:3AHQ, ECO:0007744|PDB:3AHR
ChainResidueDetails
AARG187
ATHR189
ATRP200
ASER252
AHIS255
AARG287
AARG300

site_idSWS_FT_FI2
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:24275569
ChainResidueDetails
ASER106

site_idSWS_FT_FI3
Number of Residues1
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163
ChainResidueDetails
ASER143

site_idSWS_FT_FI4
Number of Residues1
DetailsMOD_RES: Phosphoserine; by FAM20C => ECO:0000269|PubMed:29858230
ChainResidueDetails
ASER145

site_idSWS_FT_FI5
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000269|PubMed:19159218
ChainResidueDetails
AASN280

site_idSWS_FT_FI6
Number of Residues1
DetailsCARBOHYD: N-linked (GlcNAc...) asparagine => ECO:0000255
ChainResidueDetails
AASN384

226707

PDB entries from 2024-10-30

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