1EX7
CRYSTAL STRUCTURE OF YEAST GUANYLATE KINASE IN COMPLEX WITH GUANOSINE-5'-MONOPHOSPHATE
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 | 0005634 | cellular_component | nucleus |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005829 | cellular_component | cytosol |
| A | 0006163 | biological_process | purine nucleotide metabolic process |
| A | 0009150 | biological_process | purine ribonucleotide metabolic process |
| A | 0016301 | molecular_function | kinase activity |
| A | 0016740 | molecular_function | transferase activity |
| A | 0046037 | biological_process | GMP metabolic process |
| A | 0046711 | biological_process | GDP biosynthetic process |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE SO4 A 188 |
| Chain | Residue |
| A | THR12 |
| A | GLY13 |
| A | SER60 |
| A | LYS63 |
| A | ASN168 |
| A | LEU171 |
| A | HOH230 |
| A | HOH235 |
| site_id | AC2 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 189 |
| Chain | Residue |
| A | GLY11 |
| A | THR12 |
| A | GLY13 |
| A | LYS14 |
| A | SER15 |
| A | ARG135 |
| A | HOH253 |
| A | HOH329 |
| A | SER10 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE 5GP A 187 |
| Chain | Residue |
| A | SER34 |
| A | ARG38 |
| A | ARG41 |
| A | TYR50 |
| A | GLU69 |
| A | TYR78 |
| A | GLY79 |
| A | SER80 |
| A | ILE99 |
| A | ASP100 |
| A | GLY103 |
| A | HOH213 |
| A | HOH248 |
| A | HOH344 |
| A | HOH390 |
Functional Information from PROSITE/UniProt
| site_id | PS00856 |
| Number of Residues | 18 |
| Details | GUANYLATE_KINASE_1 Guanylate kinase-like signature. TTRtpRagEvnGkdYnFV |
| Chain | Residue | Details |
| A | THR36-VAL53 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 182 |
| Details | Domain: {"description":"Guanylate kinase-like","evidences":[{"source":"PROSITE-ProRule","id":"PRU00100","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 7 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00100","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"1314905","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"1967656","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"1GKY","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"1314905","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"2551688","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17287358","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"17330950","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"18407956","evidenceCode":"ECO:0007744"},{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"19779198","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
