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 R6D A 701 |
| Chain | Residue |
| A | LEU377 |
| A | GLY454 |
| A | LEU501 |
| A | ASP512 |
| A | HOH864 |
| B | ASN615 |
| A | GLY378 |
| A | VAL385 |
| A | ALA400 |
| A | LYS402 |
| A | MET448 |
| A | GLU449 |
| A | ALA451 |
| A | GLU452 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue R6D B 701 |
| Chain | Residue |
| B | LEU377 |
| B | GLY378 |
| B | PHE382 |
| B | VAL385 |
| B | ALA400 |
| B | MET448 |
| B | GLU449 |
| B | ALA451 |
| B | GLU452 |
| B | GLY454 |
| B | GLN462 |
| B | LEU501 |
| B | ASP512 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 26 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGSGNFGTVKkGyyqmkkvvkt........VAVK |
| Chain | Residue | Details |
| A | LEU377-LYS402 | |
| site_id | PS00109 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FVHrDLAARNVLL |
| Chain | Residue | Details |
| A | PHE490-LEU502 | |
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 | 18 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 11 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 5 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine; by autocatalysis","evidences":[{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"UniProtKB","id":"P48025","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"18369315","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"21469132","evidenceCode":"ECO:0000269"}]} |
