Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein 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 | 6 |
Details | BINDING SITE FOR RESIDUE PO4 A 801 |
Chain | Residue |
A | ASP595 |
A | HIS636 |
A | HIS639 |
A | ILE782 |
A | PRO783 |
A | HOH905 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 802 |
Chain | Residue |
A | GLY730 |
A | LYS616 |
A | LYS617 |
A | TYR726 |
site_id | AC3 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE PO4 A 803 |
Chain | Residue |
A | TYR554 |
A | TYR597 |
A | TYR599 |
A | PO4804 |
site_id | AC4 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE PO4 A 804 |
Chain | Residue |
A | ILE518 |
A | PHE540 |
A | TYR554 |
A | TYR599 |
A | PO4803 |
site_id | AC5 |
Number of Residues | 15 |
Details | BINDING SITE FOR RESIDUE 1PH A 805 |
Chain | Residue |
A | LYS529 |
A | SER533 |
A | GLY534 |
A | VAL539 |
A | GLN541 |
A | ALA551 |
A | LYS553 |
A | MET602 |
A | GLU603 |
A | CYS604 |
A | GLY605 |
A | ASN606 |
A | LEU654 |
A | ILE663 |
A | EDO808 |
site_id | AC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 806 |
Chain | Residue |
A | ARG523 |
A | TYR525 |
A | TYR550 |
site_id | AC7 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 807 |
Chain | Residue |
A | ASN562 |
A | ARG569 |
A | GLU633 |
A | HIS636 |
site_id | AC8 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 808 |
Chain | Residue |
A | LEU575 |
A | MET600 |
A | MET602 |
A | ILE663 |
A | 1PH805 |
A | EDO810 |
site_id | AC9 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE EDO A 809 |
Chain | Residue |
A | TYR591 |
A | ASP766 |
A | HIS788 |
A | HOH904 |
site_id | BC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 810 |
Chain | Residue |
A | LYS553 |
A | TYR568 |
A | EDO808 |
site_id | BC2 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 811 |
Chain | Residue |
A | LYS629 |
A | GLU633 |
A | EDO815 |
site_id | BC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE EDO A 812 |
Chain | Residue |
A | SER526 |
A | LEU543 |
A | CYS604 |
A | ASN606 |
A | VAL656 |
A | ASP657 |
site_id | BC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE EDO A 813 |
site_id | BC5 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 814 |
Chain | Residue |
A | LYS538 |
A | TYR554 |
A | ASN556 |
site_id | BC6 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE EDO A 815 |
Chain | Residue |
A | VAL791 |
A | GLN792 |
A | EDO811 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 23 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGSGGSSKVFqVlnekkqi...........YAIK |
Chain | Residue | Details |
A | ILE531-LYS553 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvHsDLKpaNFLI |
Chain | Residue | Details |
A | ILE643-ILE655 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP647 | |
Chain | Residue | Details |
A | ILE531 | |
A | LYS553 | |