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 | 16 |
Details | binding site for residue VX6 A 601 |
Chain | Residue |
A | LEU248 |
A | MET318 |
A | THR319 |
A | TYR320 |
A | GLY321 |
A | LEU370 |
A | HOH751 |
A | HOH767 |
A | TYR253 |
A | VAL256 |
A | ALA269 |
A | LYS271 |
A | ILE313 |
A | THR315 |
A | GLU316 |
A | PHE317 |
site_id | AC2 |
Number of Residues | 2 |
Details | binding site for residue MXE A 602 |
Chain | Residue |
A | ASP363 |
A | GLY383 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue MXE A 603 |
Chain | Residue |
A | PHE401 |
A | PRO402 |
A | ILE403 |
A | LYS404 |
A | LEU445 |
site_id | AC4 |
Number of Residues | 10 |
Details | binding site for residue VX6 B 601 |
Chain | Residue |
B | LEU248 |
B | TYR253 |
B | VAL256 |
B | ALA269 |
B | THR315 |
B | GLU316 |
B | PHE317 |
B | MET318 |
B | THR319 |
B | GLY321 |
site_id | AC5 |
Number of Residues | 8 |
Details | binding site for residue MES B 602 |
Chain | Residue |
A | GLU282 |
A | ARG362 |
A | TYR393 |
A | HOH757 |
A | HOH771 |
B | VAL338 |
B | TYR342 |
B | ASN374 |
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 | |