4E3C
X-ray crystal structure of human IKK2 in an active conformation
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 |
Functional Information from PROSITE/UniProt
| site_id | PS00108 |
| Number of Residues | 13 |
| Details | PROTEIN_KINASE_ST Serine/Threonine protein kinases active-site signature. IiHrDLKpeNIVL |
| Chain | Residue | Details |
| A | ILE141-LEU153 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 126 |
| Details | Region: {"description":"Leucine-zipper"} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 6 |
| 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_FI3 |
| Number of Residues | 54 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine; by TBK1 and PKC/PRKCZ","evidences":[{"source":"PubMed","id":"10022904","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10195894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10783893","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"S-nitrosocysteine","evidences":[{"source":"PubMed","id":"15184672","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| 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_FI7 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Phosphoserine; by TBK1, PKC/PRKCZ and PDPK1","evidences":[{"source":"PubMed","id":"10022904","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10195894","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"10783893","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"16207722","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI8 |
| Number of Residues | 6 |
| Details | Modified residue: {"description":"Hydroxyproline","evidences":[{"source":"PubMed","id":"17114296","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI9 |
| Number of Residues | 12 |
| Details | Cross-link: {"description":"Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)","evidences":[{"source":"PubMed","id":"16267042","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
