1EX6
CRYSTAL STRUCTURE OF UNLIGANDED FORM OF GUANYLATE KINASE FROM YEAST
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004385 | molecular_function | guanylate 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 | 0016301 | molecular_function | kinase activity |
A | 0016310 | biological_process | phosphorylation |
A | 0046037 | biological_process | GMP metabolic process |
A | 0046711 | biological_process | GDP biosynthetic process |
B | 0004385 | molecular_function | guanylate kinase activity |
B | 0005524 | molecular_function | ATP binding |
B | 0005634 | cellular_component | nucleus |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0006163 | biological_process | purine nucleotide metabolic process |
B | 0016301 | molecular_function | kinase activity |
B | 0016310 | biological_process | phosphorylation |
B | 0046037 | biological_process | GMP metabolic process |
B | 0046711 | biological_process | GDP biosynthetic process |
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 | 2 |
Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00100 |
Chain | Residue | Details |
A | PRO9 | |
B | PRO209 |
site_id | SWS_FT_FI2 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|PubMed:1314905, ECO:0000269|PubMed:1967656, ECO:0007744|PDB:1GKY |
Chain | Residue | Details |
A | SER35 | |
B | TRP270 | |
B | GLY279 | |
B | MET301 | |
A | THR39 | |
A | ASN51 | |
A | TRP70 | |
A | GLY79 | |
A | MET101 | |
B | SER235 | |
B | THR239 | |
B | ASN251 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | MOD_RES: N-acetylserine => ECO:0000269|PubMed:1314905, ECO:0000269|PubMed:2551688 |
Chain | Residue | Details |
A | ARG2 | |
B | ARG202 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:17287358, ECO:0007744|PubMed:17330950, ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
A | ALA149 | |
B | ALA349 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:19779198 |
Chain | Residue | Details |
A | ALA157 | |
B | ALA357 |