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 | 13 |
| Details | BINDING SITE FOR RESIDUE WTJ A 1513 |
| Chain | Residue |
| A | LEU226 |
| A | NO31515 |
| A | HOH2066 |
| A | HOH2132 |
| A | HOH2246 |
| A | ALA247 |
| A | GLU302 |
| A | LEU303 |
| A | MET304 |
| A | GLU305 |
| A | GLU351 |
| A | LEU354 |
| A | ASP368 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NO3 A 1514 |
| Chain | Residue |
| A | LEU375 |
| A | GLY403 |
| A | TYR404 |
| A | ASN405 |
| A | ARG406 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE NO3 A 1515 |
| Chain | Residue |
| A | LYS224 |
| A | LYS245 |
| A | LEU303 |
| A | WTJ1513 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE EDO A 1516 |
| Chain | Residue |
| A | GLU219 |
| A | ASN290 |
| A | PHE291 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE EDO A 1517 |
| Chain | Residue |
| A | LYS278 |
| A | ILE288 |
| A | LYS289 |
| A | ASN290 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE EDO A 1518 |
| Chain | Residue |
| A | ALA215 |
| A | PHE292 |
| site_id | AC7 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE EDO A 1519 |
| Chain | Residue |
| A | ASN269 |
| A | ARG346 |
| A | HIS371 |
| A | SER379 |
| A | ARG382 |
| A | THR383 |
| A | HOH2102 |
| A | HOH2248 |
Functional Information from PROSITE/UniProt
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpeNVLL |
| Chain | Residue | Details |
| A | ILE343-LEU355 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | Active site: {"description":"Proton acceptor"} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 9 |
| Details | Binding site: {} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"18644861","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"11390408","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17715138","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 | ASP347 | |
| A | GLU351 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP347 | |
| A | LYS349 | |
| site_id | CSA3 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP347 | |
| A | LYS349 | |
| A | THR387 | |
| site_id | CSA4 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP347 | |
| A | ASN352 | |
| A | LYS349 | |
