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 | 14 |
| Details | binding site for residue 1N1 B 601 |
| Chain | Residue |
| B | LEU267 |
| B | TYR339 |
| B | GLY340 |
| B | LEU389 |
| B | ALA399 |
| B | PHE401 |
| B | ALA288 |
| B | LYS290 |
| B | MET309 |
| B | ILE332 |
| B | THR334 |
| B | GLU335 |
| B | MET337 |
| B | THR338 |
| site_id | AC2 |
| Number of Residues | 15 |
| Details | binding site for residue 1N1 A 601 |
| Chain | Residue |
| A | LEU267 |
| A | ALA288 |
| A | LYS290 |
| A | MET309 |
| A | ILE332 |
| A | THR334 |
| A | GLU335 |
| A | PHE336 |
| A | MET337 |
| A | THR338 |
| A | GLY340 |
| A | LEU389 |
| A | ALA399 |
| A | ASP400 |
| B | LEU141 |
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 |
| B | LEU267-LYS290 | |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNCLV |
| Chain | Residue | Details |
| B | PHE378-VAL390 | |
Functional Information from SwissProt/UniProt
| Chain | Residue | Details |
| B | ASP382 | |
| A | ASP382 | |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | LEU267 | |
| B | LYS290 | |
| B | GLU335 | |
| A | LEU267 | |
| A | LYS290 | |
| A | GLU335 | |
| Chain | Residue | Details |
| B | TYR147 | |
| A | TYR234 | |
| B | TYR158 | |
| B | TYR191 | |
| B | TYR204 | |
| B | TYR234 | |
| A | TYR147 | |
| A | TYR158 | |
| A | TYR191 | |
| A | TYR204 | |
| Chain | Residue | Details |
| B | TYR245 | |
| A | TYR245 | |
| Chain | Residue | Details |
| B | SER248 | |
| A | SER248 | |
| Chain | Residue | Details |
| B | TYR272 | |
| B | TYR276 | |
| B | TYR432 | |
| A | TYR272 | |
| A | TYR276 | |
| A | TYR432 | |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036 |
| Chain | Residue | Details |
| B | TYR412 | |
| A | TYR412 | |
| Chain | Residue | Details |
| B | SER465 | |
| A | SER465 | |
