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 | Active site: {"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"15632195","evidenceCode":"ECO:0000269"}]} |
