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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 11 |
| Details | binding site for residue C2V A 401 |
| Chain | Residue |
| A | LEU20 |
| A | LEU143 |
| A | ASP157 |
| A | VAL28 |
| A | ALA41 |
| A | VAL74 |
| A | PHE90 |
| A | ASP91 |
| A | VAL93 |
| A | GLU140 |
| A | ASN141 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue DTT A 402 |
| Chain | Residue |
| A | GLN118 |
| A | ILE272 |
| A | CYS273 |
| A | GLN274 |
| A | ARG275 |
| A | SER276 |
| A | HOH623 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | binding site for residue DTT B 401 |
| Chain | Residue |
| B | GLN118 |
| B | ILE272 |
| B | CYS273 |
| B | GLN274 |
| B | ARG275 |
| B | SER276 |
| site_id | AC4 |
| Number of Residues | 13 |
| Details | binding site for residue C2V B 402 |
| Chain | Residue |
| B | LEU20 |
| B | GLY21 |
| B | VAL28 |
| B | ALA41 |
| B | PHE90 |
| B | ASP91 |
| B | LEU92 |
| B | VAL93 |
| B | GLU140 |
| B | ASN141 |
| B | LEU143 |
| B | ASP157 |
| B | HOH508 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGAFSVVRrCmkiptgqe..........YAAK |
| Chain | Residue | Details |
| A | LEU20-LYS43 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHrDLKpeNLLL |
| Chain | Residue | Details |
| A | ILE132-LEU144 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 516 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Region: {"description":"Autoinhibitory domain","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| 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_FI4 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"16690701","evidenceCode":"ECO:0000269"}]} |
