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 |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 21 |
Details | binding site for residue 66K A 601 |
Chain | Residue |
A | VAL270 |
A | GLU316 |
A | PHE317 |
A | MET318 |
A | GLY321 |
A | ILE360 |
A | HIS361 |
A | LEU370 |
A | VAL379 |
A | ALA380 |
A | ASP381 |
A | LYS271 |
A | PHE382 |
A | HOH868 |
A | GLU286 |
A | MET290 |
A | ILE293 |
A | LEU298 |
A | VAL299 |
A | ILE313 |
A | THR315 |
site_id | AC2 |
Number of Residues | 13 |
Details | binding site for residue 66K A 602 |
Chain | Residue |
A | MET226 |
A | PRO309 |
A | PHE311 |
A | ARG386 |
A | LEU387 |
A | MET388 |
A | ILE403 |
A | ALA412 |
A | TYR449 |
A | GLU453 |
A | HOH758 |
A | HOH760 |
A | HOH776 |
site_id | AC3 |
Number of Residues | 5 |
Details | binding site for residue EDO A 603 |
Chain | Residue |
A | TYR253 |
A | ASN322 |
A | ARG367 |
A | HIS396 |
A | HOH857 |
site_id | AC4 |
Number of Residues | 5 |
Details | binding site for residue EDO A 604 |
Chain | Residue |
A | GLU238 |
A | ARG457 |
A | ARG473 |
A | TRP476 |
A | GLN477 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue EDO A 605 |
Chain | Residue |
A | MET244 |
A | TYR257 |
A | TYR312 |
site_id | AC6 |
Number of Residues | 7 |
Details | binding site for residue EDO A 606 |
Chain | Residue |
A | LYS234 |
A | TRP235 |
A | MET237 |
A | TRP261 |
A | LEU302 |
A | HOH739 |
A | HOH784 |
site_id | AC7 |
Number of Residues | 4 |
Details | binding site for residue EDO A 607 |
Chain | Residue |
A | ALA337 |
A | TYR435 |
A | HOH711 |
A | HOH728 |
site_id | AC8 |
Number of Residues | 5 |
Details | binding site for residue EDO A 608 |
Chain | Residue |
A | ASN336 |
A | GLU494 |
A | HOH705 |
A | HOH710 |
A | HOH736 |
site_id | AC9 |
Number of Residues | 1 |
Details | binding site for residue EDO A 609 |
site_id | AD1 |
Number of Residues | 4 |
Details | binding site for residue EDO A 610 |
Chain | Residue |
A | ILE360 |
A | PHE416 |
A | SER417 |
A | HOH805 |
site_id | AD2 |
Number of Residues | 6 |
Details | binding site for residue EDO A 611 |
Chain | Residue |
A | TYR326 |
A | GLU329 |
A | CYS330 |
A | EDO612 |
A | HOH791 |
A | HOH895 |
site_id | AD3 |
Number of Residues | 6 |
Details | binding site for residue EDO A 612 |
Chain | Residue |
A | TYR320 |
A | TYR326 |
A | GLU334 |
A | ASN374 |
A | EDO611 |
A | HOH815 |
site_id | AD4 |
Number of Residues | 3 |
Details | binding site for residue EDO A 613 |
Chain | Residue |
A | GLN498 |
A | HOH786 |
A | HOH836 |
site_id | AD5 |
Number of Residues | 1 |
Details | binding site for residue EDO A 614 |
site_id | AD6 |
Number of Residues | 3 |
Details | binding site for residue CL A 615 |
Chain | Residue |
A | LYS274 |
A | GLU275 |
A | ASP276 |
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 | |
site_id | SWS_FT_FI2 |
Number of Residues | 3 |
Details | BINDING: |
Chain | Residue | Details |
A | LEU248 | |
A | LYS271 | |
A | GLU316 | |
Chain | Residue | Details |
A | SER229 | |
Chain | Residue | Details |
A | TYR253 | |
A | TYR257 | |
A | TYR413 | |
site_id | SWS_FT_FI5 |
Number of Residues | 1 |
Details | MOD_RES: Phosphotyrosine; by autocatalysis and SRC-type Tyr-kinases => ECO:0000269|PubMed:16912036 |
Chain | Residue | Details |
A | TYR393 | |
Chain | Residue | Details |
A | SER446 | |