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 | 8 | 
| Details | BINDING SITE FOR RESIDUE 1AW A 1 | 
| Chain | Residue | 
| A | GLU310 | 
| A | MET314 | 
| A | LEU317 | 
| A | LEU322 | 
| A | VAL402 | 
| A | ALA403 | 
| A | ASP404 | 
| A | PHE405 | 
| site_id | AC2 | 
| Number of Residues | 13 | 
| Details | BINDING SITE FOR RESIDUE 1AW A 534 | 
| Chain | Residue | 
| A | GLY274 | 
| A | GLN275 | 
| A | GLY276 | 
| A | GLY279 | 
| A | VAL281 | 
| A | ALA293 | 
| A | TYR340 | 
| A | MET341 | 
| A | CYS345 | 
| A | ASP348 | 
| A | PHE405 | 
| B | HOH61 | 
| A | LEU273 | 
| site_id | AC3 | 
| Number of Residues | 8 | 
| Details | BINDING SITE FOR RESIDUE 1AW B 1 | 
| Chain | Residue | 
| B | LYS295 | 
| B | GLU310 | 
| B | MET314 | 
| B | LEU317 | 
| B | VAL402 | 
| B | ALA403 | 
| B | ASP404 | 
| B | GLY406 | 
Functional Information from PROSITE/UniProt
| site_id | PS00107 | 
| Number of Residues | 23 | 
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGCFGEVWmGtwngttr...........VAIK | 
| Chain | Residue | Details | 
| A | LEU273-LYS295 |  | 
| site_id | PS00109 | 
| Number of Residues | 13 | 
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. YVHrDLRAANILV | 
| Chain | Residue | Details | 
| A | TYR382-VAL394 |  | 
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 | 
| Number of Residues | 2 | 
| 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_FI2 | 
| Number of Residues | 16 | 
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} | 
| site_id | SWS_FT_FI3 | 
| Number of Residues | 2 | 
| Details | Binding site: {} | 
| site_id | SWS_FT_FI4 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"8856081","evidenceCode":"ECO:0000269"}]} | 
| site_id | SWS_FT_FI5 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"19948721","evidenceCode":"ECO:0000269"}]} | 
| site_id | SWS_FT_FI6 | 
| Number of Residues | 2 | 
| Details | Modified residue: {"description":"Phosphotyrosine; by CSK","evidences":[{"source":"PubMed","id":"2420005","evidenceCode":"ECO:0000269"}]} | 
Catalytic Information from CSA
| site_id | CSA1 | 
| Number of Residues | 2 | 
| Details | Annotated By Reference To The Literature 1ir3 | 
| Chain | Residue | Details | 
| A | ASP386 |  | 
| A | ALA390 |  | 
| site_id | CSA2 | 
| Number of Residues | 2 | 
| Details | Annotated By Reference To The Literature 1ir3 | 
| Chain | Residue | Details | 
| B | ASP386 |  | 
| B | ALA390 |  | 
| site_id | CSA3 | 
| Number of Residues | 2 | 
| Details | Annotated By Reference To The Literature 1ir3 | 
| Chain | Residue | Details | 
| A | ARG388 |  | 
| A | ASP386 |  | 
| site_id | CSA4 | 
| Number of Residues | 2 | 
| Details | Annotated By Reference To The Literature 1ir3 | 
| Chain | Residue | Details | 
| B | ARG388 |  | 
| B | ASP386 |  | 
| site_id | CSA5 | 
| Number of Residues | 3 | 
| Details | Annotated By Reference To The Literature 1ir3 | 
| Chain | Residue | Details | 
| A | ARG388 |  | 
| A | ASN391 |  | 
| A | ASP386 |  | 
| site_id | CSA6 | 
| Number of Residues | 3 | 
| Details | Annotated By Reference To The Literature 1ir3 | 
| Chain | Residue | Details | 
| B | ARG388 |  | 
| B | ASN391 |  | 
| B | ASP386 |  |