Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0004385 | molecular_function | GMP kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006163 | biological_process | purine nucleotide metabolic process |
| A | 0009179 | biological_process | purine ribonucleoside diphosphate metabolic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0042802 | molecular_function | identical protein binding |
| A | 0046037 | biological_process | GMP metabolic process |
| A | 0046710 | biological_process | GDP metabolic process |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0004385 | molecular_function | GMP kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005829 | cellular_component | cytosol |
| B | 0006163 | biological_process | purine nucleotide metabolic process |
| B | 0009179 | biological_process | purine ribonucleoside diphosphate metabolic process |
| B | 0016301 | molecular_function | kinase activity |
| B | 0016740 | molecular_function | transferase activity |
| B | 0042802 | molecular_function | identical protein binding |
| B | 0046037 | biological_process | GMP metabolic process |
| B | 0046710 | biological_process | GDP metabolic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE K A 603 |
| Chain | Residue |
| A | SER38 |
| A | ASP102 |
| A | GDP601 |
| A | HOH623 |
| A | HOH625 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE K B 1603 |
| Chain | Residue |
| B | HOH1605 |
| B | HOH1638 |
| B | SER38 |
| B | ASP102 |
| B | GDP1601 |
| B | HOH1604 |
| site_id | AC3 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE GDP A 601 |
| Chain | Residue |
| A | SER18 |
| A | SER38 |
| A | ARG42 |
| A | ARG45 |
| A | TYR54 |
| A | GLU73 |
| A | VAL77 |
| A | TYR82 |
| A | GLY83 |
| A | THR84 |
| A | ASP102 |
| A | ILE103 |
| A | ASP104 |
| A | GLY107 |
| A | K603 |
| A | HOH631 |
| A | HOH640 |
| A | HOH645 |
| A | HOH657 |
| A | HOH662 |
| A | HOH684 |
| site_id | AC4 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GMP A 602 |
| Chain | Residue |
| A | LEU30 |
| A | TYR31 |
| A | GLN34 |
| A | THR95 |
| A | VAL97 |
| A | ARG133 |
| A | ARG134 |
| A | GLY137 |
| A | ARG138 |
| A | HOH615 |
| A | HOH626 |
| A | HOH634 |
| site_id | AC5 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE GDP B 1601 |
| Chain | Residue |
| B | SER38 |
| B | ARG42 |
| B | ARG45 |
| B | TYR54 |
| B | GLU73 |
| B | TYR82 |
| B | GLY83 |
| B | THR84 |
| B | ASP102 |
| B | ILE103 |
| B | ASP104 |
| B | GLY107 |
| B | K1603 |
| B | HOH1637 |
| B | HOH1675 |
| B | HOH1676 |
| B | HOH1698 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GMP B 1602 |
| Chain | Residue |
| B | TYR31 |
| B | GLN34 |
| B | THR95 |
| B | VAL97 |
| B | ARG133 |
| B | ARG134 |
| B | GLY137 |
| B | ARG138 |
| B | HOH1624 |
| B | HOH1631 |
| B | HOH1670 |
| B | HOH1684 |
Functional Information from PROSITE/UniProt
| site_id | PS00856 |
| Number of Residues | 18 |
| Details | GUANYLATE_KINASE_1 Guanylate kinase-like signature. TTRqpRpgEvhGehYfFV |
| Chain | Residue | Details |
| A | THR40-VAL57 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 360 |
| Details | Domain: {"description":"Guanylate kinase-like"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 14 |
| Details | Binding site: {"evidences":[{"evidenceCode":"ECO:0000250"}]} |
