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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 627 A 1504 |
| Chain | Residue |
| A | LEU248 |
| A | ARG367 |
| A | LEU370 |
| A | HOH2006 |
| A | HOH2104 |
| A | GLY250 |
| A | ALA269 |
| A | LYS271 |
| A | GLU316 |
| A | PHE317 |
| A | MET318 |
| A | THR319 |
| A | GLY321 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE 627 B 1504 |
| Chain | Residue |
| B | LEU248 |
| B | GLY250 |
| B | ALA269 |
| B | LYS271 |
| B | GLU316 |
| B | PHE317 |
| B | MET318 |
| B | THR319 |
| B | GLY321 |
| B | ARG367 |
| B | LEU370 |
| B | ASP381 |
| B | HOH2062 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MG A 1505 |
| Chain | Residue |
| A | ASN368 |
| A | ASP381 |
| A | HOH2054 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG B 1505 |
| Chain | Residue |
| B | ASN368 |
| B | ASP381 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGGGQYGEVYeGvwkkyslt..........VAVK |
| Chain | Residue | Details |
| A | LEU248-LYS271 | |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNCLV |
| Chain | Residue | Details |
| A | PHE359-VAL371 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| A | ASP363 | |
| B | ASP363 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLU316 | |
| B | LEU248 | |
| B | LYS271 | |
| B | GLU316 | |
| A | LEU248 | |
| A | LYS271 | |
| Chain | Residue | Details |
| A | SER229 | |
| B | SER229 | |
| Chain | Residue | Details |
| A | TYR413 | |
| B | TYR253 | |
| B | TYR257 | |
| B | TYR413 | |
| A | TYR253 | |
| A | TYR257 | |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036 |
| Chain | Residue | Details |
| A | PTR393 | |
| B | PTR393 | |
| Chain | Residue | Details |
| A | SER446 | |
| B | SER446 | |
