Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004672 | molecular_function | protein kinase activity |
A | 0004674 | molecular_function | protein serine/threonine kinase activity |
A | 0004697 | molecular_function | diacylglycerol-dependent serine/threonine kinase activity |
A | 0005524 | molecular_function | ATP binding |
A | 0006468 | biological_process | protein phosphorylation |
B | 0004672 | molecular_function | protein kinase activity |
B | 0004674 | molecular_function | protein serine/threonine kinase activity |
B | 0004697 | molecular_function | diacylglycerol-dependent serine/threonine 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 | 14 |
Details | BINDING SITE FOR RESIDUE PDS A 901 |
Chain | Residue |
A | HOH57 |
A | ASP470 |
A | ASN471 |
A | MET473 |
A | ALA483 |
A | ASP484 |
A | LEU348 |
A | PHE353 |
A | VAL356 |
A | ALA369 |
A | THR404 |
A | GLU421 |
A | TYR422 |
A | VAL423 |
site_id | AC2 |
Number of Residues | 13 |
Details | BINDING SITE FOR RESIDUE PDS B 902 |
Chain | Residue |
B | HOH59 |
B | LEU348 |
B | VAL356 |
B | ALA369 |
B | THR404 |
B | MET420 |
B | GLU421 |
B | TYR422 |
B | VAL423 |
B | ASP470 |
B | ASN471 |
B | ALA483 |
B | ASP484 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 24 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGSFGKVMlSerkgtdel..........YAVK |
Chain | Residue | Details |
A | LEU348-LYS371 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiYrDLKldNVML |
Chain | Residue | Details |
A | ILE462-LEU474 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | LEU467 | |
B | LEU467 | |
Chain | Residue | Details |
A | GLY349 | |
A | ILE372 | |
B | GLY349 | |
B | ILE372 | |
Chain | Residue | Details |
A | VAL325 | |
B | VAL325 | |
Chain | Residue | Details |
A | PHE501 | |
B | PHE501 | |
Chain | Residue | Details |
A | PRO505 | |
B | PRO505 | |
Chain | Residue | Details |
A | HIS636 | |
B | HIS636 | |
Chain | Residue | Details |
A | PRO643 | |
B | PRO643 | |
Chain | Residue | Details |
A | VAL662 | |
B | VAL662 | |
Chain | Residue | Details |
A | ASN663 | |
B | ASN663 | |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP466 | |
A | ASP470 | |
site_id | CSA2 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP466 | |
B | ASP470 | |
site_id | CSA3 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP466 | |
A | LYS468 | |
site_id | CSA4 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP466 | |
B | LYS468 | |
site_id | CSA5 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | THR504 | |
A | ASP466 | |
A | LYS468 | |
site_id | CSA6 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | THR504 | |
B | ASP466 | |
B | LYS468 | |
site_id | CSA7 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
A | ASP466 | |
A | LYS468 | |
A | ASN471 | |
site_id | CSA8 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1ir3 |
Chain | Residue | Details |
B | ASP466 | |
B | LYS468 | |
B | ASN471 | |