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 | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 336 |
| Chain | Residue |
| A | VAL11 |
| A | HIS148 |
| A | ALA315 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 337 |
| Chain | Residue |
| A | ARG155 |
| A | GLU180 |
| site_id | AC3 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 338 |
| Chain | Residue |
| A | PRO159 |
| A | HIS160 |
| site_id | AC4 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE ANP A 339 |
| Chain | Residue |
| A | GLY48 |
| A | TYR50 |
| A | SER51 |
| A | VAL53 |
| A | ALA66 |
| A | LYS68 |
| A | GLU114 |
| A | VAL116 |
| A | ASN118 |
| A | HIS160 |
| A | LEU163 |
| A | ASP175 |
| A | HOH370 |
| A | HOH403 |
| A | HOH503 |
| A | HOH559 |
| A | HOH576 |
| A | LEU45 |
| A | ARG47 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 340 |
| Chain | Residue |
| A | ARG21 |
| A | LEU41 |
| A | ASP103 |
| A | PRO104 |
| A | HOH432 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 336 |
| Chain | Residue |
| B | HIS148 |
| B | ALA315 |
| B | HOH350 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 337 |
| Chain | Residue |
| B | ARG155 |
| B | ASN189 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL B 338 |
| Chain | Residue |
| B | LYS68 |
| B | PHE113 |
| B | ASP175 |
| B | ANP339 |
| B | HOH353 |
| B | HOH553 |
| site_id | AC9 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE ANP B 339 |
| Chain | Residue |
| B | GLY46 |
| B | ARG47 |
| B | GLY48 |
| B | SER51 |
| B | VAL53 |
| B | ALA66 |
| B | LYS68 |
| B | ILE95 |
| B | PHE113 |
| B | GLU114 |
| B | VAL116 |
| B | ASN118 |
| B | ASP120 |
| B | HIS160 |
| B | LEU163 |
| B | ASP175 |
| B | CL338 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 340 |
| Chain | Residue |
| B | PRO20 |
| B | ARG21 |
| B | LEU41 |
| B | PRO104 |
| B | HOH347 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGRGKYSEVFeAinitnnek..........VAVK |
| Chain | Residue | Details |
| A | LEU45-LYS68 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ImHrDVKphNVLI |
| Chain | Residue | Details |
| A | ILE152-ILE164 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 570 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 10 |
| Details | Region: {"description":"Interaction with beta subunit","evidences":[{"evidenceCode":"ECO:0000250"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor"} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 18 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP156 | |
| A | HIS160 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP156 | |
| B | HIS160 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP156 | |
| A | LYS158 | |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP156 | |
| B | LYS158 | |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP156 | |
| A | LYS158 | |
| A | SER194 | |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP156 | |
| B | LYS158 | |
| B | SER194 | |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP156 | |
| A | ASN161 | |
| A | LYS158 | |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP156 | |
| B | ASN161 | |
| B | LYS158 | |
