7YAW
Crystal structure of ZAK in complex with compound YH-180
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PROSITE/UniProt
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHrDLKsrNVVI |
| Chain | Residue | Details |
| D | VAL129-ILE141 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250|UniProtKB:P80192, ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| D | ASP133 | |
| A | ASP133 | |
| B | ASP133 | |
| C | ASP133 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P80192, ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| D | CYS22 | |
| A | CYS22 | |
| B | CYS22 | |
| C | CYS22 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000269|PubMed:11836244 |
| Chain | Residue | Details |
| D | LYS45 | |
| A | LYS45 | |
| B | LYS45 | |
| C | LYS45 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:32289254 |
| Chain | Residue | Details |
| D | SER7 | |
| A | SER7 | |
| B | SER7 | |
| C | SER7 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000269|PubMed:15342622, ECO:0000269|PubMed:26999302 |
| Chain | Residue | Details |
| D | THR161 | |
| A | THR161 | |
| B | THR161 | |
| C | THR161 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:15342622, ECO:0000269|PubMed:26999302 |
| Chain | Residue | Details |
| D | SER165 | |
| A | SER165 | |
| B | SER165 | |
| C | SER165 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine => ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195 |
| Chain | Residue | Details |
| D | SER275 | |
| A | SER275 | |
| B | SER275 | |
| C | SER275 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphoserine; by autocatalysis => ECO:0000269|PubMed:32289254, ECO:0007744|PubMed:18691976 |
| Chain | Residue | Details |
| D | SER302 | |
| A | SER302 | |
| B | SER302 | |
| C | SER302 |
