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 | 5 |
| Details | BINDING SITE FOR RESIDUE MG A 401 |
| Chain | Residue |
| A | SER14 |
| A | SER14 |
| A | PHE17 |
| A | PHE17 |
| A | LEU18 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE Q1A A 402 |
| Chain | Residue |
| A | VAL76 |
| A | MET92 |
| A | GLU93 |
| A | TYR94 |
| A | MET95 |
| A | LEU145 |
| A | ALA155 |
| A | ASP156 |
| A | LEU157 |
| A | ILE43 |
| A | GLU63 |
| A | MET67 |
| A | LEU70 |
| site_id | AC3 |
| Number of Residues | 14 |
| Details | BINDING SITE FOR RESIDUE Q1A B 401 |
| Chain | Residue |
| B | ILE43 |
| B | GLU63 |
| B | MET66 |
| B | MET67 |
| B | LEU70 |
| B | VAL75 |
| B | VAL76 |
| B | MET92 |
| B | GLU93 |
| B | TYR94 |
| B | MET95 |
| B | LEU145 |
| B | ALA155 |
| B | ASP156 |
Functional Information from PROSITE/UniProt
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. ViHkDLKpeNILV |
| Chain | Residue | Details |
| A | VAL134-VAL146 | |
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"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by IKKA and IKKB","evidences":[{"source":"PubMed","id":"18408713","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine; by IKKA and IKKB","evidences":[{"source":"PubMed","id":"18408713","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"30988283","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine; by RIPK3 and autocatalysis","evidences":[{"evidenceCode":"ECO:0000255"}]} |
| site_id | SWS_FT_FI7 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"18408713","evidenceCode":"ECO:0000269"}]} |
