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1QVZ

Crystal structure of the S. cerevisiae YDR533c protein

Functional Information from GO Data
ChainGOidnamespacecontents
A0000932cellular_componentP-body
A0005737cellular_componentcytoplasm
A0006457biological_processprotein folding
A0010494cellular_componentcytoplasmic stress granule
A0016829molecular_functionlyase activity
A0019172molecular_functionglyoxalase III activity
A0019243biological_processmethylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione
A0019249biological_processlactate biosynthetic process
A0031669biological_processcellular response to nutrient levels
A0034599biological_processcellular response to oxidative stress
A0044183molecular_functionprotein folding chaperone
B0000932cellular_componentP-body
B0005737cellular_componentcytoplasm
B0006457biological_processprotein folding
B0010494cellular_componentcytoplasmic stress granule
B0016829molecular_functionlyase activity
B0019172molecular_functionglyoxalase III activity
B0019243biological_processmethylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione
B0019249biological_processlactate biosynthetic process
B0031669biological_processcellular response to nutrient levels
B0034599biological_processcellular response to oxidative stress
B0044183molecular_functionprotein folding chaperone
Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues6
DetailsACT_SITE: ACT_SITE => ECO:0000305|PubMed:14745011, ECO:0000305|PubMed:15130476
ChainResidueDetails
ACSO138
AHIS139
AGLU170
BCSO138
BHIS139
BGLU170

site_idSWS_FT_FI2
Number of Residues2
DetailsMOD_RES: Cysteine sulfinic acid (-SO2H) => ECO:0000269|PubMed:14745011
ChainResidueDetails
ACSO138
BCSO138

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PDB entries from 2025-07-02

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