3UOW
Crystal Structure of PF10_0123, a GMP Synthetase from Plasmodium Falciparum
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0003921 | molecular_function | GMP synthase activity |
| A | 0003922 | molecular_function | GMP synthase (glutamine-hydrolyzing) activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005829 | cellular_component | cytosol |
| A | 0006164 | biological_process | purine nucleotide biosynthetic process |
| A | 0006177 | biological_process | GMP biosynthetic process |
| A | 0006541 | biological_process | glutamine metabolic process |
| A | 0016874 | molecular_function | ligase activity |
| A | 0046037 | biological_process | GMP metabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0003921 | molecular_function | GMP synthase activity |
| B | 0003922 | molecular_function | GMP synthase (glutamine-hydrolyzing) activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005829 | cellular_component | cytosol |
| B | 0006164 | biological_process | purine nucleotide biosynthetic process |
| B | 0006177 | biological_process | GMP biosynthetic process |
| B | 0006541 | biological_process | glutamine metabolic process |
| B | 0016874 | molecular_function | ligase activity |
| B | 0046037 | biological_process | GMP metabolic process |
| B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE XMP A 556 |
| Chain | Residue |
| A | ARG336 |
| A | HOH561 |
| A | PRO434 |
| A | GLY435 |
| A | PRO436 |
| A | GLN476 |
| A | LYS547 |
| A | THR551 |
| A | ILE552 |
| A | GLU553 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CA A 557 |
| Chain | Residue |
| A | ASP355 |
| A | ASN422 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE XMP B 556 |
| Chain | Residue |
| B | ARG336 |
| B | PRO434 |
| B | GLY435 |
| B | PRO436 |
| B | GLN476 |
| B | LYS547 |
| B | THR551 |
| B | ILE552 |
| B | GLU553 |
| B | HOH564 |
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 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00886 |
| Chain | Residue | Details |
| A | SER262 | |
| B | SER262 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|Ref.6, ECO:0007744|PDB:3UOW |
| Chain | Residue | Details |
| A | ARG336 | |
| A | GLN476 | |
| A | LYS547 | |
| A | ILE552 | |
| A | GLU553 | |
| B | ARG336 | |
| B | GLN476 | |
| B | LYS547 | |
| B | ILE552 | |
| B | GLU553 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | SITE: Important for ATPPase activity => ECO:0000269|PubMed:32358899 |
| Chain | Residue | Details |
| A | ASP371 | |
| A | HIS388 | |
| A | HIS389 | |
| B | ASP371 | |
| B | HIS388 | |
| B | HIS389 |
