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 | 17 |
Details | BINDING SITE FOR RESIDUE P16 A 532 |
Chain | Residue |
A | TYR272 |
A | MET337 |
A | THR338 |
A | GLY340 |
A | LEU389 |
A | ALA399 |
A | ASP400 |
A | PHE401 |
A | HOH646 |
A | ALA288 |
A | VAL289 |
A | LYS290 |
A | MET309 |
A | ILE332 |
A | THR334 |
A | GLU335 |
A | PHE336 |
site_id | AC2 |
Number of Residues | 16 |
Details | BINDING SITE FOR RESIDUE P16 B 532 |
Chain | Residue |
B | TYR272 |
B | ALA288 |
B | LYS290 |
B | GLU305 |
B | MET309 |
B | ILE332 |
B | THR334 |
B | GLU335 |
B | PHE336 |
B | MET337 |
B | GLY340 |
B | LEU389 |
B | ALA399 |
B | ASP400 |
B | PHE401 |
B | HOH664 |
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 | LEU267 | |
A | LYS290 | |
A | GLU335 | |
B | LEU267 | |
B | LYS290 | |
B | GLU335 | |
Chain | Residue | Details |
A | SER248 | |
B | SER248 | |
Chain | Residue | Details |
A | TYR272 | |
A | TYR276 | |
A | TYR432 | |
B | TYR272 | |
B | TYR276 | |
B | TYR432 | |
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 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ARG386 | |
A | ASP382 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ARG386 | |
B | ASP382 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ALA384 | |
A | ASP382 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ALA384 | |
B | ASP382 | |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ALA384 | |
A | ASP382 | |
A | ASN387 | |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ALA384 | |
B | ASP382 | |
B | ASN387 | |