Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A1335 |
| Chain | Residue |
| A | GLN101 |
| A | HOH2032 |
| A | HOH2052 |
| A | HOH2053 |
| A | HOH2071 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE MG A1336 |
| Chain | Residue |
| A | HOH2122 |
| A | ASP162 |
| A | ASP185 |
| A | HOH2107 |
| A | HOH2114 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A1337 |
| Chain | Residue |
| A | LYS137 |
| A | TYR317 |
| A | MET318 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A1338 |
| Chain | Residue |
| A | LYS61 |
| A | ARG149 |
| site_id | AC5 |
| Number of Residues | 15 |
| Details | BINDING SITE FOR RESIDUE BRQ A1334 |
| Chain | Residue |
| A | ILE49 |
| A | ASN53 |
| A | LEU57 |
| A | LYS72 |
| A | LEU116 |
| A | GLU117 |
| A | LEU118 |
| A | LEU119 |
| A | GLY120 |
| A | PRO121 |
| A | ILE184 |
| A | PRO331 |
| A | THR332 |
| A | PRO333 |
| A | HOH2237 |
| site_id | AC6 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE PGO A1339 |
| Chain | Residue |
| A | GLY50 |
| A | GLY120 |
| A | SER122 |
| A | ASP125 |
| A | LEU169 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGCGNFGELRlGknlytney..........VAIK |
| Chain | Residue | Details |
| A | ILE49-LYS72 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LiYrDVKpeNFLI |
| Chain | Residue | Details |
| A | LEU158-ILE170 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 270 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 9 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"20068231","evidenceCode":"ECO:0007744"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | GLU166 | |
| A | ASP162 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS164 | |
| A | ASP162 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR212 | |
| A | LYS164 | |
| A | ASP162 | |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | LYS164 | |
| A | ASN167 | |
| A | ASP162 | |
