4WIN
Crystal structure of the GATase domain from Plasmodium falciparum 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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | binding site for residue NO3 A 1001 |
| Chain | Residue |
| A | ASN13 |
| A | PHE19 |
| A | THR35 |
| B | ASN13 |
| B | PHE19 |
| B | THR35 |
| B | LYS36 |
| B | ASP37 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue NO3 A 1002 |
| Chain | Residue |
| A | GLN17 |
| A | TYR18 |
| A | GLY57 |
| A | GLY58 |
| A | HIS208 |
| B | TYR60 |
| A | SER16 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | binding site for residue NO3 B 301 |
| Chain | Residue |
| A | TYR60 |
| B | SER16 |
| B | GLN17 |
| B | GLY58 |
| B | HIS208 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile; for GATase activity => ECO:0000255|PROSITE-ProRule:PRU00605, ECO:0000305|PubMed:21413787, ECO:0000305|PubMed:26592566 |
| Chain | Residue | Details |
| A | CYS89 | |
| B | CYS89 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: For GATase activity => ECO:0000255|PROSITE-ProRule:PRU00605 |
| Chain | Residue | Details |
| A | HIS208 | |
| A | GLU210 | |
| B | HIS208 | |
| B | GLU210 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:26592566, ECO:0007744|PDB:4WIO |
| Chain | Residue | Details |
| A | GLN93 | |
| A | ASN169 | |
| A | ASP172 | |
| A | HIS208 | |
| B | GLN93 | |
| B | ASN169 | |
| B | ASP172 | |
| B | HIS208 |
