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2FA4

Crystal Structure of Oxidized Form from Saccharomyces cerevisiae

Functional Information from GO Data
ChainGOidnamespacecontents
A0000011biological_processvacuole inheritance
A0000103biological_processsulfate assimilation
A0000139cellular_componentGolgi membrane
A0000324cellular_componentfungal-type vacuole
A0005515molecular_functionprotein binding
A0005634cellular_componentnucleus
A0005737cellular_componentcytoplasm
A0005794cellular_componentGolgi apparatus
A0005829cellular_componentcytosol
A0006749biological_processglutathione metabolic process
A0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
A0006890biological_processretrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
A0009263biological_processdeoxyribonucleotide biosynthetic process
A0015031biological_processprotein transport
A0015035molecular_functionprotein-disulfide reductase activity
A0015036molecular_functiondisulfide oxidoreductase activity
A0016020cellular_componentmembrane
A0042144biological_processvacuole fusion, non-autophagic
A0045454biological_processcell redox homeostasis
A0120124cellular_componentmembrane fusion priming complex
B0000011biological_processvacuole inheritance
B0000103biological_processsulfate assimilation
B0000139cellular_componentGolgi membrane
B0000324cellular_componentfungal-type vacuole
B0005515molecular_functionprotein binding
B0005634cellular_componentnucleus
B0005737cellular_componentcytoplasm
B0005794cellular_componentGolgi apparatus
B0005829cellular_componentcytosol
B0006749biological_processglutathione metabolic process
B0006888biological_processendoplasmic reticulum to Golgi vesicle-mediated transport
B0006890biological_processretrograde vesicle-mediated transport, Golgi to endoplasmic reticulum
B0009263biological_processdeoxyribonucleotide biosynthetic process
B0015031biological_processprotein transport
B0015035molecular_functionprotein-disulfide reductase activity
B0015036molecular_functiondisulfide oxidoreductase activity
B0016020cellular_componentmembrane
B0042144biological_processvacuole fusion, non-autophagic
B0045454biological_processcell redox homeostasis
B0120124cellular_componentmembrane fusion priming complex
Functional Information from PROSITE/UniProt
site_idPS00194
Number of Residues19
DetailsTHIOREDOXIN_1 Thioredoxin family active site. VVdFFatWCGPCKmIapmI
ChainResidueDetails
AVAL23-ILE41

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues4
DetailsACT_SITE: Nucleophile
ChainResidueDetails
ACYS31
ACYS34
BCYS31
BCYS34

site_idSWS_FT_FI2
Number of Residues2
DetailsSITE: Deprotonates C-terminal active site Cys
ChainResidueDetails
AASP25
BASP25

site_idSWS_FT_FI3
Number of Residues4
DetailsSITE: Contributes to redox potential value
ChainResidueDetails
AGLY32
APRO33
BGLY32
BPRO33

site_idSWS_FT_FI4
Number of Residues2
DetailsMOD_RES: Phosphoserine => ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198
ChainResidueDetails
ASER62
BSER62

site_idSWS_FT_FI5
Number of Residues6
DetailsCROSSLNK: Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) => ECO:0007744|PubMed:22106047
ChainResidueDetails
ALYS67
ALYS97
BLYS67
BLYS97

Catalytic Information from CSA
site_idCSA1
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
ACYS31
ACYS34
APRO33
AGLY32

site_idCSA2
Number of Residues4
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
BCYS31
BCYS34
BPRO33
BGLY32

site_idCSA3
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
ACYS31
ACYS34

site_idCSA4
Number of Residues2
DetailsAnnotated By Reference To The Literature 1mek
ChainResidueDetails
BCYS31
BCYS34

237735

PDB entries from 2025-06-18

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