Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0006751 | biological_process | glutathione catabolic process |
A | 0036374 | molecular_function | glutathione hydrolase activity |
C | 0006751 | biological_process | glutathione catabolic process |
C | 0036374 | molecular_function | glutathione hydrolase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE AVN B 390 |
Chain | Residue |
A | ARG114 |
B | MET464 |
B | GLY484 |
B | HOH611 |
B | HOH692 |
B | THR391 |
B | THR409 |
B | ASN411 |
B | GLN430 |
B | ASP433 |
B | TYR444 |
B | SER462 |
B | SER463 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE AVN D 390 |
Chain | Residue |
C | ARG114 |
D | THR391 |
D | THR409 |
D | ASN411 |
D | GLN430 |
D | ASP433 |
D | TYR444 |
D | SER462 |
D | SER463 |
D | MET464 |
D | GLY484 |
D | HOH628 |
D | HOH684 |
Functional Information from PROSITE/UniProt
site_id | PS00462 |
Number of Residues | 25 |
Details | G_GLU_TRANSPEPTIDASE Gamma-glutamyltranspeptidase signature. TTHySVvdkdGNaVAvTyTLNttFG |
Chain | Residue | Details |
B | THR391-GLY415 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 10 |
Details | Binding site: {"evidences":[{"source":"PubMed","id":"16618936","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 38 |
Details | Region: {"description":"Disordered","evidences":[{"source":"SAM","id":"MobiDB-lite","evidenceCode":"ECO:0000256"}]} |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | Active site: {"description":"Nucleophile","evidences":[{"source":"PubMed","id":"16618936","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18555071","evidenceCode":"ECO:0000269"}]} |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | Binding site: {} |