2V36
Crystal structure of gamma-glutamyl transferase from Bacillus subtilis
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006751 | biological_process | glutathione catabolic process |
| A | 0036374 | molecular_function | glutathione hydrolase activity |
| B | 0006751 | biological_process | glutathione catabolic process |
| B | 0036374 | molecular_function | glutathione hydrolase activity |
| C | 0006751 | biological_process | glutathione catabolic process |
| C | 0036374 | molecular_function | glutathione hydrolase activity |
| D | 0006751 | biological_process | glutathione catabolic process |
| D | 0036374 | molecular_function | glutathione hydrolase activity |
Functional Information from PROSITE/UniProt
| site_id | PS00462 |
| Number of Residues | 25 |
| Details | G_GLU_TRANSPEPTIDASE Gamma-glutamyltranspeptidase signature. TTHfTVadrwGNvVSyTtTIEqlFG |
| Chain | Residue | Details |
| B | THR403-GLY427 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000305|PubMed:20088880 |
| Chain | Residue | Details |
| B | THR403 | |
| D | THR403 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250 |
| Chain | Residue | Details |
| B | THR421 | |
| D | THR421 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20088880 |
| Chain | Residue | Details |
| B | GLU423 | |
| B | GLU442 | |
| B | ASP445 | |
| D | GLU423 | |
| D | GLU442 | |
| D | ASP445 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:20088880, ECO:0007744|PDB:3A75 |
| Chain | Residue | Details |
| B | SER464 | |
| B | GLY485 | |
| D | SER464 | |
| D | GLY485 |
