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 | 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 | 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 401 |
Chain | Residue |
A | LYS113 |
A | HOH513 |
A | HOH581 |
A | HOH591 |
A | ARG115 |
A | GLY193 |
A | ARG197 |
A | CYS234 |
A | ARG247 |
A | HIS250 |
A | ZN403 |
A | HOH509 |
site_id | AC2 |
Number of Residues | 20 |
Details | binding site for residue ANP A 402 |
Chain | Residue |
A | GLY80 |
A | GLY82 |
A | SER83 |
A | PHE84 |
A | VAL87 |
A | ALA103 |
A | LYS105 |
A | ASP153 |
A | LEU155 |
A | LYS200 |
A | GLU202 |
A | ASN203 |
A | LEU205 |
A | THR215 |
A | LYS221 |
A | HOH514 |
A | HOH535 |
A | HOH537 |
A | HOH560 |
A | HOH586 |
site_id | AC3 |
Number of Residues | 3 |
Details | binding site for residue ZN A 403 |
Chain | Residue |
A | CYS234 |
A | HIS250 |
A | ANP401 |
site_id | AC4 |
Number of Residues | 14 |
Details | binding site for residue ANP B 401 |
Chain | Residue |
B | LYS113 |
B | GLY193 |
B | VAL195 |
B | ARG197 |
B | CYS234 |
B | ARG247 |
B | HIS250 |
B | ZN403 |
B | HOH506 |
B | HOH511 |
B | HOH513 |
B | HOH523 |
B | HOH526 |
B | HOH591 |
site_id | AC5 |
Number of Residues | 3 |
Details | binding site for residue ZN B 403 |
Chain | Residue |
B | CYS234 |
B | HIS250 |
B | ANP401 |
site_id | AC6 |
Number of Residues | 24 |
Details | binding site for Di-peptide ANP B 402 and LYS B 200 |
Chain | Residue |
B | GLY80 |
B | GLN81 |
B | GLY82 |
B | SER83 |
B | PHE84 |
B | VAL87 |
B | ALA103 |
B | LYS105 |
B | ASP153 |
B | LEU155 |
B | ASP198 |
B | LEU199 |
B | PRO201 |
B | GLU202 |
B | ASN203 |
B | ILE204 |
B | LEU205 |
B | THR215 |
B | LYS221 |
B | HOH514 |
B | HOH517 |
B | HOH542 |
B | HOH548 |
B | HOH575 |
Functional Information from PROSITE/UniProt
site_id | PS00107 |
Number of Residues | 27 |
Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGQGSFGKVFlVrkktgpdagql.......YAMK |
Chain | Residue | Details |
A | LEU79-LYS105 | |
site_id | PS00108 |
Number of Residues | 13 |
Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IvYrDLKpeNILL |
Chain | Residue | Details |
A | ILE194-LEU206 | |
site_id | PS00284 |
Number of Residues | 11 |
Details | SERPIN Serpins signature. VEVNHPFIVkL |
Chain | Residue | Details |
A | VAL128-LEU138 | |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000250 |
Chain | Residue | Details |
A | ASP198 | |
B | ASP198 | |
Chain | Residue | Details |
A | LEU79 | |
A | LYS105 | |
B | LEU79 | |
B | LYS105 | |
Chain | Residue | Details |
A | SER232 | |
B | SER232 | |