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 | 9 |
| Details | BINDING SITE FOR RESIDUE SO4 A 801 |
| Chain | Residue |
| A | HOH101 |
| A | PRO152 |
| A | TYR153 |
| A | LYS154 |
| A | ASP155 |
| A | PHE232 |
| A | ASN233 |
| A | HIS234 |
| A | LYS235 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 B 802 |
| Chain | Residue |
| B | PRO152 |
| B | LYS154 |
| B | ASP155 |
| B | ASN233 |
| B | HIS234 |
| B | LYS235 |
| site_id | AC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE EDO A 1000 |
| Chain | Residue |
| A | ALA198 |
| A | ASP201 |
| A | GLY552 |
| A | ALA554 |
| A | TYR561 |
| A | MOH2390 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE EDO B 1003 |
| Chain | Residue |
| A | HOH34 |
| B | ALA198 |
| B | ASP201 |
| B | GLY552 |
| B | ALA554 |
| B | TYR561 |
| B | MOH2389 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE MOH B 2389 |
| Chain | Residue |
| A | GLU197 |
| A | MOH2390 |
| B | EDO1003 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MOH A 2390 |
| Chain | Residue |
| A | EDO1000 |
| B | MOH2389 |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGWGHFSTVWlAkdmvnnth..........VAMK |
| Chain | Residue | Details |
| A | LEU164-LYS187 | |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHtDIKpeNVLM |
| Chain | Residue | Details |
| A | ILE290-MET302 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI2 |
| 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 | GLU298 | |
| A | ASP294 | |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | GLU298 | |
| B | ASP294 | |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP294 | |
| A | LYS296 | |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP294 | |
| B | LYS296 | |
| site_id | CSA5 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | THR567 | |
| A | ASP294 | |
| A | LYS296 | |
| site_id | CSA6 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | THR567 | |
| B | ASP294 | |
| B | LYS296 | |
| site_id | CSA7 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| A | ASP294 | |
| A | LYS296 | |
| A | ASN299 | |
| site_id | CSA8 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1ir3 |
| Chain | Residue | Details |
| B | ASP294 | |
| B | LYS296 | |
| B | ASN299 | |
