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 | 20 |
| Details | binding site for residue ANP A 501 |
| Chain | Residue |
| A | GLY156 |
| A | ASP279 |
| A | ASN280 |
| A | ASP294 |
| A | MG502 |
| A | MG503 |
| A | HOH613 |
| A | HOH614 |
| A | HOH615 |
| A | HOH620 |
| A | HOH621 |
| A | ALA157 |
| A | HOH645 |
| A | PHE158 |
| A | LYS159 |
| A | VAL161 |
| A | GLU228 |
| A | MET230 |
| A | ASP275 |
| A | LYS277 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | binding site for residue MG A 502 |
| Chain | Residue |
| A | ASN280 |
| A | ASP294 |
| A | ANP501 |
| A | HOH615 |
| A | HOH645 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue MG A 503 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | binding site for residue EDO A 504 |
| Chain | Residue |
| A | SER143 |
| A | ARG145 |
| A | GLU168 |
| A | ARG412 |
| A | GLU414 |
| site_id | AC5 |
| Number of Residues | 22 |
| Details | binding site for residue ANP B 501 |
| Chain | Residue |
| B | GLY156 |
| B | ALA157 |
| B | PHE158 |
| B | LYS159 |
| B | VAL161 |
| B | GLU228 |
| B | LEU229 |
| B | MET230 |
| B | ASP275 |
| B | LYS277 |
| B | ASP279 |
| B | ASN280 |
| B | PHE282 |
| B | ASP294 |
| B | MG502 |
| B | MG503 |
| B | HOH602 |
| B | HOH608 |
| B | HOH622 |
| B | HOH629 |
| B | HOH645 |
| B | HOH653 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue MG B 502 |
| Chain | Residue |
| B | ASP279 |
| B | ASN280 |
| B | ASP294 |
| B | ANP501 |
| B | HOH602 |
| B | HOH629 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | binding site for residue MG B 503 |
| Chain | Residue |
| B | LYS277 |
| B | ANP501 |
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 | ILE271-ILE283 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"UniProtKB","id":"Q9JIH7","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"UniProtKB","id":"Q9H4A3","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"UniProtKB","id":"Q9JIH7","evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"33439774","evidenceCode":"ECO:0000269"}]} |
