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 | 19 |
Details | BINDING SITE FOR RESIDUE ANP A 1000 |
Chain | Residue |
A | GLU329 |
A | GLU396 |
A | LEU398 |
A | LEU447 |
A | ASP458 |
A | PHE459 |
A | GLY460 |
A | PHE461 |
A | HOH1118 |
A | HOH1119 |
A | HOH1125 |
A | GLY330 |
A | SER331 |
A | THR332 |
A | VAL335 |
A | ALA348 |
A | LYS350 |
A | GLU366 |
A | MET395 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE ANP B 1000 |
Chain | Residue |
B | GLU329 |
B | GLY330 |
B | SER331 |
B | THR332 |
B | VAL335 |
B | ALA348 |
B | LYS350 |
B | GLU366 |
B | MET395 |
B | GLU396 |
B | PHE397 |
B | LEU398 |
B | LEU447 |
B | ASP458 |
B | PHE459 |
B | GLY460 |
B | PHE461 |
B | HOH1118 |
B | HOH1119 |
B | HOH1130 |
site_id | AC3 |
Number of Residues | 13 |
Details | BINDING SITE FOR CHAIN C OF SERINE/THREONINE-PROTEIN KINASE PAK 4 |
Chain | Residue |
A | SER331 |
A | GLN358 |
A | ARG359 |
A | THR404 |
A | SER443 |
A | ASP444 |
A | PHE461 |
A | LEU475 |
A | VAL476 |
A | GLY477 |
A | TYR480 |
A | TRP481 |
A | GLU507 |
site_id | AC4 |
Number of Residues | 12 |
Details | BINDING SITE FOR CHAIN D OF SERINE/THREONINE-PROTEIN KINASE PAK 4 |
Chain | Residue |
B | SER331 |
B | ARG359 |
B | THR404 |
B | ASP444 |
B | LEU475 |
B | VAL476 |
B | GLY477 |
B | PRO479 |
B | TYR480 |
B | TRP481 |
B | GLU507 |
B | PHE516 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 25 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGEGSTGIVCiAtvrssgklv.........AVKK |
Chain | Residue | Details |
A | ILE327-LYS351 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP440 | |
B | ASP440 | |
Chain | Residue | Details |
B | ILE327 | |
B | LYS350 | |
A | ILE327 | |
A | LYS350 | |
Chain | Residue | Details |
B | GLU396 | |
B | ASP458 | |
A | GLU396 | |
A | ASP458 | |
Chain | Residue | Details |
A | PRO314 | |
B | PRO314 | |
Chain | Residue | Details |
A | LYS351 | |
B | LYS351 | |
Chain | Residue | Details |
A | ASP440 | |
A | LEU531 | |
A | SER291 | |
B | ASN377 | |
B | CYS421 | |
B | ASP440 | |
B | LEU531 | |
B | SER291 | |
A | ASN377 | |
A | CYS421 | |
Chain | Residue | Details |
A | VAL454 | |
B | VAL454 | |
Chain | Residue | Details |
A | GLY460 | |
B | GLY460 | |
Chain | Residue | Details |
A | GLU468 | |
B | GLU468 | |
Chain | Residue | Details |
A | TYR480 | |
B | TYR480 | |
Chain | Residue | Details |
A | LYS540 | |
B | LYS540 | |
Chain | Residue | Details |
A | SEP474 | |
B | SEP474 | |