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 | 24 |
| Details | BINDING SITE FOR RESIDUE 406 A 1001 |
| Chain | Residue |
| A | HOH9 |
| A | MET290 |
| A | ILE293 |
| A | LEU298 |
| A | VAL299 |
| A | ILE313 |
| A | THR315 |
| A | PHE317 |
| A | MET318 |
| A | ILE360 |
| A | HIS361 |
| A | HOH16 |
| A | ARG362 |
| A | VAL379 |
| A | ALA380 |
| A | ASP381 |
| A | PHE382 |
| A | HOH102 |
| A | LEU248 |
| A | TYR253 |
| A | ALA269 |
| A | LYS271 |
| A | GLU286 |
| A | VAL289 |
| site_id | AC2 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE 406 B 1002 |
| Chain | Residue |
| B | HOH33 |
| B | LEU248 |
| B | TYR253 |
| B | ALA269 |
| B | LYS271 |
| B | GLU286 |
| B | VAL289 |
| B | MET290 |
| B | ILE293 |
| B | LEU298 |
| B | VAL299 |
| B | ILE313 |
| B | THR315 |
| B | PHE317 |
| B | MET318 |
| B | LEU354 |
| B | ILE360 |
| B | HIS361 |
| B | ARG362 |
| B | VAL379 |
| B | ALA380 |
| B | ASP381 |
| B | PHE382 |
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 | LEU248 | |
| A | LYS271 | |
| A | GLU316 | |
| B | LEU248 | |
| B | LYS271 | |
| B | GLU316 | |
| Chain | Residue | Details |
| A | SER229 | |
| B | SER229 | |
| Chain | Residue | Details |
| A | TYR253 | |
| A | TYR257 | |
| A | TYR413 | |
| B | TYR253 | |
| B | TYR257 | |
| B | TYR413 | |
| 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 | TYR393 | |
| B | TYR393 | |
| Chain | Residue | Details |
| A | SER446 | |
| B | SER446 | |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP363 | |
| A | ARG367 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP363 | |
| B | ARG367 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP363 | |
| A | ALA365 | |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP363 | |
| B | ALA365 | |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASN368 | |
| A | ASP363 | |
| A | ALA365 | |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASN368 | |
| B | ASP363 | |
| B | ALA365 | |
