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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A1384 |
| Chain | Residue |
| A | HIS173 |
| A | SER236 |
| A | SER237 |
| A | PRO331 |
| A | HOH2105 |
| A | HOH2106 |
| A | HOH2107 |
| A | HOH2108 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A1385 |
| Chain | Residue |
| A | PHE360 |
| A | LEU359 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A1386 |
| Chain | Residue |
| A | ASP264 |
| A | HOH2109 |
| A | HOH2110 |
| A | HOH2111 |
| A | HOH2112 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A1387 |
| Chain | Residue |
| A | ARG96 |
| A | ARG180 |
| A | LYS205 |
| A | ASN213 |
| A | VAL214 |
| A | GLU290 |
| A | PHE291 |
| A | HOH2087 |
| site_id | AC5 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE BRW A1383 |
| Chain | Residue |
| A | ILE62 |
| A | ALA83 |
| A | ASP133 |
| A | TYR134 |
| A | VAL135 |
| A | PRO136 |
| A | ARG141 |
| A | LEU188 |
| A | ASP200 |
| A | HOH2019 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 25 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. IGNGSFGVVYqAklcdsgelv.........AIKK |
| Chain | Residue | Details |
| A | ILE62-LYS86 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IcHrDIKpqNLLL |
| Chain | Residue | Details |
| A | ILE177-LEU189 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 284 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor"} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"17050006","evidenceCode":"ECO:0000305"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphotyrosine","evidences":[{"source":"PubMed","id":"12554650","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"25169422","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP181 | |
| A | GLN185 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP181 | |
| A | LYS183 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP181 | |
| A | LYS183 | |
| A | SER219 | |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP181 | |
| A | ASN186 | |
| A | LYS183 | |
