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 | 12 |
Details | binding site for residue ANP A 501 |
Chain | Residue |
A | GLY230 |
A | LYS375 |
A | HOH621 |
A | HOH671 |
A | SER231 |
A | PHE232 |
A | LYS233 |
A | VAL235 |
A | THR301 |
A | GLU302 |
A | MET304 |
A | PHE356 |
site_id | AC2 |
Number of Residues | 11 |
Details | binding site for residue ANP B 501 |
Chain | Residue |
B | GLY230 |
B | SER231 |
B | PHE232 |
B | LYS233 |
B | VAL235 |
B | ALA248 |
B | THR301 |
B | GLU302 |
B | HOH624 |
B | HOH636 |
B | HOH712 |
Functional Information from PROSITE/UniProt
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKcdNIFI |
Chain | Residue | Details |
A | ILE345-ILE357 | |
Functional Information from SwissProt/UniProt
Chain | Residue | Details |
A | ASP368 | |
B | ASP368 | |
Chain | Residue | Details |
A | LYS351 | |
B | SER231 | |
B | THR301 | |
B | LYS351 | |
A | SER231 | |
A | THR301 | |
Chain | Residue | Details |
B | PHE283 | |
B | LEU299 | |
B | LEU369 | |
B | LEU371 | |
A | LEU369 | |
A | LEU371 | |
A | PHE283 | |
A | LEU299 | |
Chain | Residue | Details |
A | SER378 | |
B | SER378 | |
Chain | Residue | Details |
A | SEP382 | |
B | SEP382 | |