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 |
B | 0004672 | molecular_function | protein 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 MG A 1739 |
Chain | Residue |
A | ASN299 |
A | ASP550 |
A | HOH2013 |
site_id | AC2 |
Number of Residues | 9 |
Details | BINDING SITE FOR RESIDUE SO4 A 1740 |
Chain | Residue |
A | LYS235 |
A | HOH2054 |
A | HOH2055 |
A | TYR153 |
A | LYS154 |
A | ASP155 |
A | PHE232 |
A | ASN233 |
A | HIS234 |
site_id | AC3 |
Number of Residues | 10 |
Details | BINDING SITE FOR RESIDUE SO4 B 1738 |
Chain | Residue |
B | PRO152 |
B | TYR153 |
B | LYS154 |
B | ASP155 |
B | PHE232 |
B | ASN233 |
B | HIS234 |
B | LYS235 |
B | HOH2077 |
B | HOH2078 |
site_id | AC4 |
Number of Residues | 1 |
Details | BINDING SITE FOR RESIDUE MG B 1739 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGWGHFSTVWlAkdmvnnth..........VAMK |
Chain | Residue | Details |
A | LEU164-LYS187 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHtDIKpeNVLM |
Chain | Residue | Details |
A | ILE290-MET302 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
site_id | SWS_FT_FI2 |
Number of Residues | 18 |
Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | GLU298 | |
A | ASP294 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | GLU298 | |
B | ASP294 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP294 | |
A | LYS296 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP294 | |
B | LYS296 | |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | THR567 | |
A | ASP294 | |
A | LYS296 | |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | THR567 | |
B | ASP294 | |
B | LYS296 | |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP294 | |
A | LYS296 | |
A | ASN299 | |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP294 | |
B | LYS296 | |
B | ASN299 | |