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 | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 4 |
Chain | Residue |
A | ARG479 |
A | GLU481 |
A | GLY482 |
site_id | AC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 A 5 |
Chain | Residue |
A | HOH21 |
A | ARG492 |
A | GLN496 |
site_id | AC3 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE STI A 3 |
Chain | Residue |
A | GLU305 |
A | MET309 |
A | ILE312 |
A | VAL318 |
A | THR334 |
A | PHE336 |
A | MET337 |
A | ILE379 |
A | HIS380 |
A | ARG381 |
A | ALA399 |
A | ASP400 |
A | PHE401 |
A | HOH33 |
A | ALA288 |
A | LYS290 |
site_id | AC4 |
Number of Residues | 11 |
Details | BINDING SITE FOR RESIDUE 3YY A 538 |
Chain | Residue |
A | HOH150 |
A | ALA356 |
A | LEU359 |
A | ALA363 |
A | LEU448 |
A | ILE451 |
A | ALA452 |
A | GLU481 |
A | GLY482 |
A | CYS483 |
A | PRO484 |
site_id | AC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE SO4 B 3 |
Chain | Residue |
A | GLU469 |
A | LYS473 |
B | LYS313 |
site_id | AC6 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE STI B 4 |
Chain | Residue |
B | HOH177 |
B | TYR272 |
B | LYS290 |
B | GLU305 |
B | MET309 |
B | ILE312 |
B | VAL318 |
B | ILE332 |
B | THR334 |
B | PHE336 |
B | MET337 |
B | ILE379 |
B | HIS380 |
B | ALA399 |
B | ASP400 |
B | PHE401 |
site_id | AC7 |
Number of Residues | 8 |
Details | BINDING SITE FOR RESIDUE 2PE B 170 |
Chain | Residue |
B | ASN355 |
B | VAL358 |
B | TYR361 |
B | ASN393 |
B | TYR432 |
B | LYS434 |
B | PHE516 |
B | SER520 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE GOL B 60 |
Chain | Residue |
B | HOH37 |
B | ASP474 |
B | ARG476 |
B | ARG492 |
B | TRP495 |
B | GLN496 |
site_id | AC9 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE 3YY B 532 |
Chain | Residue |
A | GLU392 |
A | ASN393 |
B | HOH152 |
B | ALA356 |
B | LEU359 |
B | ALA363 |
B | LEU448 |
B | ILE451 |
B | ALA452 |
B | GLU481 |
B | GLY482 |
B | CYS483 |
B | PRO484 |
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 | |
site_id | PS00109 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_TYR Tyrosine protein kinases specific active-site signature. FIHrDLAARNCLV |
Chain | Residue | Details |
A | PHE378-VAL390 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP382 | |
B | ASP382 | |
site_id | SWS_FT_FI2 |
Number of Residues | 6 |
Details | BINDING: |
Chain | Residue | Details |
A | GLU335 | |
B | LEU267 | |
B | LYS290 | |
B | GLU335 | |
A | LEU267 | |
A | LYS290 | |
Chain | Residue | Details |
A | SER248 | |
B | SER248 | |
Chain | Residue | Details |
A | TYR432 | |
B | TYR272 | |
B | TYR276 | |
B | TYR432 | |
A | TYR272 | |
A | TYR276 | |
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 | TYR412 | |
B | TYR412 | |
Chain | Residue | Details |
A | SER465 | |
B | SER465 | |