Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004713 | molecular_function | protein tyrosine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004713 | molecular_function | protein tyrosine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004713 | molecular_function | protein tyrosine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 1 |
| Chain | Residue |
| A | ILE449 |
| A | THR452 |
| A | LEU498 |
| A | HOH2004 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE VX6 A 547 |
| Chain | Residue |
| A | GLU362 |
| A | TYR363 |
| A | MET364 |
| A | PRO365 |
| A | GLY367 |
| A | LEU416 |
| A | ASP427 |
| A | TYR299 |
| A | VAL302 |
| A | ALA315 |
| A | LYS317 |
| A | THR361 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL A 548 |
| Chain | Residue |
| A | LEU294 |
| A | GLY295 |
| A | GLY297 |
| A | GLN298 |
| A | TYR299 |
| A | GLY300 |
| site_id | AC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NA A 549 |
| Chain | Residue |
| A | ARG503 |
| A | ARG519 |
| A | TRP522 |
| A | HOH2006 |
| site_id | AC5 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE VX6 B 547 |
| Chain | Residue |
| B | LEU294 |
| B | TYR299 |
| B | THR361 |
| B | GLU362 |
| B | TYR363 |
| B | MET364 |
| B | PRO365 |
| B | GLY367 |
| B | LEU416 |
| B | ASP427 |
| C | ARG374 |
| site_id | AC6 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE VX6 B 548 |
| Chain | Residue |
| A | LYS280 |
| A | TRP281 |
| A | TRP307 |
| A | TYR310 |
| A | LEU312 |
| A | LEU348 |
| B | THR352 |
| B | LEU353 |
| B | GLU354 |
| B | PRO355 |
| B | PHE357 |
| site_id | AC7 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE VX6 B 549 |
| Chain | Residue |
| B | ASP437 |
| B | THR438 |
| B | TYR459 |
| B | THR461 |
| B | SER463 |
| B | LYS465 |
| B | ALA527 |
| B | HOH2007 |
| C | VX6548 |
| site_id | AC8 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE VX6 C 547 |
| Chain | Residue |
| C | LEU294 |
| C | TYR299 |
| C | VAL302 |
| C | ALA315 |
| C | THR361 |
| C | GLU362 |
| C | TYR363 |
| C | MET364 |
| C | PRO365 |
| C | TYR366 |
| C | GLY367 |
| C | LEU416 |
| C | ASP427 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE VX6 C 548 |
| Chain | Residue |
| B | SER525 |
| B | VX6549 |
| C | THR352 |
| C | LEU353 |
| C | GLU354 |
| C | PRO355 |
| site_id | BC1 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE VX6 C 549 |
| Chain | Residue |
| B | MET483 |
| C | ALA445 |
| C | LYS446 |
| C | PHE447 |
| C | ILE449 |
| C | SER492 |
| C | TYR495 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGQYGEVYvGvwkkyslt..........VAVK |
| Chain | Residue | Details |
| A | LEU294-LYS317 | |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNCLV |
| Chain | Residue | Details |
| A | PHE405-VAL417 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 72 |
| Details | Motif: {"description":"Kinase activation loop","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10028","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 45 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 9 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P00519","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases","evidences":[{"source":"PubMed","id":"12748290","evidenceCode":"ECO:0000269"}]} |
