Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue NIL A 601 |
| Chain | Residue |
| A | TYR272 |
| A | ILE332 |
| A | ILE334 |
| A | PHE336 |
| A | MET337 |
| A | PHE378 |
| A | HIS380 |
| A | LEU389 |
| A | ALA399 |
| A | ASP400 |
| A | PHE401 |
| A | ALA288 |
| A | HOH872 |
| A | LYS290 |
| A | GLU305 |
| A | VAL308 |
| A | MET309 |
| A | ILE312 |
| A | LEU317 |
| A | VAL318 |
| site_id | AC2 |
| Number of Residues | 17 |
| Details | binding site for residue AY7 A 602 |
| Chain | Residue |
| A | ALA356 |
| A | LEU359 |
| A | LEU360 |
| A | ALA363 |
| A | LEU448 |
| A | ILE451 |
| A | ALA452 |
| A | THR453 |
| A | GLU481 |
| A | VAL487 |
| A | PHE512 |
| A | ILE521 |
| A | VAL525 |
| A | HOH715 |
| A | HOH768 |
| A | HOH866 |
| A | HOH874 |
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 | LEU267-LYS290 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 90 |
| Details | Domain: {"description":"SH2","evidences":[{"source":"PROSITE-ProRule","id":"PRU00191","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| 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 | 15 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"16912036","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"18775435","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"16912036","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"16912036","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P42684","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"23186163","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"UniProtKB","id":"P00520","evidenceCode":"ECO:0000250"}]} |
