5EBZ
Crystal structure of human IKK1
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 |
| E | 0004672 | molecular_function | protein kinase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006468 | biological_process | protein phosphorylation |
| F | 0004672 | molecular_function | protein kinase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006468 | biological_process | protein phosphorylation |
| G | 0004672 | molecular_function | protein kinase activity |
| G | 0005524 | molecular_function | ATP binding |
| G | 0006468 | biological_process | protein phosphorylation |
| H | 0004672 | molecular_function | protein kinase activity |
| H | 0005524 | molecular_function | ATP binding |
| H | 0006468 | biological_process | protein phosphorylation |
| I | 0004672 | molecular_function | protein kinase activity |
| I | 0005524 | molecular_function | ATP binding |
| I | 0006468 | biological_process | protein phosphorylation |
| J | 0004672 | molecular_function | protein kinase activity |
| J | 0005524 | molecular_function | ATP binding |
| J | 0006468 | biological_process | protein phosphorylation |
| K | 0004672 | molecular_function | protein kinase activity |
| K | 0005524 | molecular_function | ATP binding |
| K | 0006468 | biological_process | protein phosphorylation |
| L | 0004672 | molecular_function | protein kinase activity |
| L | 0005524 | molecular_function | ATP binding |
| L | 0006468 | biological_process | protein phosphorylation |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGTGGFGNVClYqhreldlk..........IAIK |
| Chain | Residue | Details |
| A | LEU21-LYS44 |
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpeNIVL |
| Chain | Residue | Details |
| A | ILE140-LEU152 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3444 |
| Details | Domain: {"description":"Protein kinase","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 252 |
| Details | Region: {"description":"Leucine-zipper"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"},{"source":"PROSITE-ProRule","id":"PRU10027","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 108 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphothreonine; by PKB/AKT1 and SGK1","evidences":[{"source":"PubMed","id":"10485710","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"19088076","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphoserine; by MAP3K14","evidences":[{"source":"PubMed","id":"9520446","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI7 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"(Microbial infection) O-acetylthreonine; by Yersinia YopJ","evidences":[{"source":"PubMed","id":"17116858","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 12 |
| Details | Modified residue: {"description":"Phosphoserine; by SGK1","evidences":[{"source":"PubMed","id":"19088076","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
