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 |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue CJJ A 301 |
| Chain | Residue |
| A | ILE19 |
| A | ASN146 |
| A | LEU148 |
| A | THR158 |
| A | ASP159 |
| A | ALA20 |
| A | VAL27 |
| A | ALA40 |
| A | LYS42 |
| A | MET95 |
| A | GLU96 |
| A | VAL98 |
| A | GLY100 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue 0BD A 302 |
| Chain | Residue |
| A | HIS117 |
| A | ASP120 |
| A | ILE149 |
| A | PRO151 |
| A | THR152 |
| A | GLY153 |
| site_id | AC3 |
| Number of Residues | 15 |
| Details | binding site for residue CJJ B 300 |
| Chain | Residue |
| B | ILE19 |
| B | ALA20 |
| B | GLY22 |
| B | VAL27 |
| B | ALA40 |
| B | LYS42 |
| B | MET95 |
| B | GLU96 |
| B | VAL98 |
| B | GLY100 |
| B | PRO102 |
| B | ASN146 |
| B | LEU148 |
| B | THR158 |
| B | ASP159 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue CJJ C 300 |
| Chain | Residue |
| C | ILE19 |
| C | ALA20 |
| C | VAL27 |
| C | ALA40 |
| C | LYS42 |
| C | GLU96 |
| C | VAL98 |
| C | GLY100 |
| C | PRO102 |
| C | GLY145 |
| C | ASN146 |
| C | LEU148 |
| C | THR158 |
| C | ASP159 |
| site_id | AC5 |
| Number of Residues | 13 |
| Details | binding site for residue CJJ D 300 |
| Chain | Residue |
| D | ILE19 |
| D | ALA20 |
| D | GLY22 |
| D | ALA40 |
| D | LYS42 |
| D | MET95 |
| D | GLU96 |
| D | VAL98 |
| D | GLY100 |
| D | GLY145 |
| D | ASN146 |
| D | LEU148 |
| D | THR158 |
Functional Information from PROSITE/UniProt
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. LvHrDVKpgNILI |
| Chain | Residue | Details |
| A | LEU137-ILE149 | |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| 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 | 36 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 40 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"25586004","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 24 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"source":"PubMed","id":"25586004","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | Modified residue: {"description":"Phosphothreonine; by autocatalysis","evidences":[{"source":"PubMed","id":"25665034","evidenceCode":"ECO:0000269"}]} |
