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 | 8 |
| Details | binding site for residue GOL A 501 |
| Chain | Residue |
| A | LYS45 |
| A | CYS62 |
| A | THR113 |
| A | ASP180 |
| A | LEU183 |
| A | HOH651 |
| A | HOH661 |
| A | HOH700 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 502 |
| Chain | Residue |
| A | TYR234 |
| A | VAL247 |
| A | GLY250 |
| A | ILE272 |
| A | GLN274 |
| A | HOH613 |
| A | TYR218 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | binding site for residue GOL A 503 |
| Chain | Residue |
| A | ARG273 |
| A | TYR280 |
| A | HOH607 |
| A | HOH695 |
| A | HOH718 |
| A | HOH729 |
| B | GLN88 |
| site_id | AC4 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 501 |
| Chain | Residue |
| B | LYS163 |
| B | CYS164 |
| B | PHE201 |
| B | MSE222 |
| B | CYS223 |
| B | GLU226 |
| B | PRO233 |
| B | HOH640 |
| B | HOH662 |
| site_id | AC5 |
| Number of Residues | 9 |
| Details | binding site for residue GOL B 502 |
| Chain | Residue |
| B | ALA60 |
| B | CYS62 |
| B | VAL93 |
| B | THR113 |
| B | GLU114 |
| B | MSE116 |
| B | PHE168 |
| B | ASP180 |
| B | GOL505 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | binding site for residue GOL B 503 |
| Chain | Residue |
| B | LYS78 |
| B | SER98 |
| B | HOH647 |
| site_id | AC7 |
| Number of Residues | 7 |
| Details | binding site for residue GOL B 504 |
| Chain | Residue |
| A | PHE191 |
| A | ALA240 |
| A | HOH609 |
| B | THR102 |
| B | VAL103 |
| B | LYS104 |
| B | HOH613 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | binding site for residue GOL B 505 |
| Chain | Residue |
| B | VAL93 |
| B | PHE95 |
| B | LEU111 |
| B | THR113 |
| B | ILE178 |
| B | GLY179 |
| B | ASP180 |
| B | LEU181 |
| B | GOL502 |
| B | HOH633 |
| B | HOH691 |
| site_id | AC9 |
| Number of Residues | 7 |
| Details | binding site for residue SO4 B 506 |
| Chain | Residue |
| B | ARG127 |
| B | PRO156 |
| B | ILE158 |
| B | ARG160 |
| B | HOH610 |
| B | HOH638 |
| B | HOH708 |
Functional Information from PROSITE/UniProt
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKcdNIFI |
| Chain | Residue | Details |
| A | ILE157-ILE169 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PubMed","id":"10828064","evidenceCode":"ECO:0000305"},{"source":"PubMed","id":"16083423","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9H4A3","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"24803536","evidenceCode":"ECO:0000305"},{"source":"PDB","id":"4Q2A","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"12374799","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"12374799","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"22544747","evidenceCode":"ECO:0000269"}]} |
