1QVW
Crystal structure of the S. cerevisiae YDR533c protein
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000932 | cellular_component | P-body |
| A | 0006457 | biological_process | protein folding |
| A | 0010494 | cellular_component | cytoplasmic stress granule |
| A | 0019172 | molecular_function | glyoxalase III activity |
| A | 0031669 | biological_process | cellular response to nutrient levels |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0044183 | molecular_function | protein folding chaperone |
| A | 0051596 | biological_process | methylglyoxal catabolic process |
| B | 0000932 | cellular_component | P-body |
| B | 0006457 | biological_process | protein folding |
| B | 0010494 | cellular_component | cytoplasmic stress granule |
| B | 0019172 | molecular_function | glyoxalase III activity |
| B | 0031669 | biological_process | cellular response to nutrient levels |
| B | 0034599 | biological_process | cellular response to oxidative stress |
| B | 0044183 | molecular_function | protein folding chaperone |
| B | 0051596 | biological_process | methylglyoxal catabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL B 501 |
| Chain | Residue |
| B | GLY52 |
| B | ALA129 |
| B | ASN130 |
| B | LYS150 |
| B | LYS151 |
| B | HOH620 |
| B | HOH635 |
| B | HOH685 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | Active site: {"evidences":[{"source":"PubMed","id":"14745011","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"15130476","evidenceCode":"ECO:0000305"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Cysteine sulfinic acid (-SO2H)","evidences":[{"source":"PubMed","id":"14745011","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
