8GR3
Crystal structure of K151L/Y158F mutant of GATase subunit of Methanocaldococcus jannaschii GMP synthetase
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003922 | molecular_function | GMP synthase (glutamine-hydrolyzing) activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006177 | biological_process | GMP biosynthetic process |
| B | 0003922 | molecular_function | GMP synthase (glutamine-hydrolyzing) activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006177 | biological_process | GMP biosynthetic process |
| C | 0003922 | molecular_function | GMP synthase (glutamine-hydrolyzing) activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006177 | biological_process | GMP biosynthetic process |
| D | 0003922 | molecular_function | GMP synthase (glutamine-hydrolyzing) activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006177 | biological_process | GMP biosynthetic process |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 748 |
| Details | Domain: {"description":"Glutamine amidotransferase type-1","evidences":[{"source":"HAMAP-Rule","id":"MF_01510","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | Active site: {"description":"Nucleophile","evidences":[{"source":"HAMAP-Rule","id":"MF_01510","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Active site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01510","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
