6EGE
Crystal structure of the unphosphorylated IRAK4 kinase domain Bound to a type I inhibitor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000287 | molecular_function | magnesium ion binding |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0004674 | molecular_function | protein serine/threonine kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| A | 0007165 | biological_process | signal transduction |
| D | 0000287 | molecular_function | magnesium ion binding |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0004674 | molecular_function | protein serine/threonine kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
| D | 0007165 | biological_process | signal transduction |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 14 |
| Details | binding site for residue DL1 D 501 |
| Chain | Residue |
| D | MET192 |
| D | LEU318 |
| D | SER328 |
| D | ASP329 |
| D | HOH664 |
| D | HOH683 |
| D | PHE197 |
| D | ALA211 |
| D | TYR262 |
| D | VAL263 |
| D | TYR264 |
| D | MET265 |
| D | GLY268 |
| D | ASP272 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue DL1 A 501 |
| Chain | Residue |
| A | MET192 |
| A | ALA211 |
| A | TYR262 |
| A | VAL263 |
| A | TYR264 |
| A | MET265 |
| A | PRO266 |
| A | GLY268 |
| A | ASP278 |
| A | ASN316 |
| A | LEU318 |
| A | SER328 |
| A | ASP329 |
| A | HOH669 |
| A | HOH702 |
| D | HOH636 |
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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 10 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17312103","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2006","submissionDatabase":"PDB data bank","title":"Crystal structures of the apo and inhibited IRAK4 kinase domain.","authors":["Mol C.D.","Arduini R.M.","Baker D.P.","Chien E.Y.","Dougan D.R.","Friedman J.","Gibaja V.","Hession C.A.","Horne A."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI5 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphothreonine","evidences":[{"source":"PubMed","id":"17161373","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17312103","evidenceCode":"ECO:0000269"},{"source":"Reference","evidenceCode":"ECO:0000269","citation":{"citationType":"submission","publicationDate":"DEC-2006","submissionDatabase":"PDB data bank","title":"Crystal structures of the apo and inhibited IRAK4 kinase domain.","authors":["Mol C.D.","Arduini R.M.","Baker D.P.","Chien E.Y.","Dougan D.R.","Friedman J.","Gibaja V.","Hession C.A.","Horne A."]}}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 1 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17161373","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17312103","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
