6O94
Structure of the IRAK4 kinase domain with compound 17
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 |
| B | 0000287 | molecular_function | magnesium ion binding |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0004674 | molecular_function | protein serine/threonine kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| B | 0007165 | biological_process | signal transduction |
| C | 0000287 | molecular_function | magnesium ion binding |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0004674 | molecular_function | protein serine/threonine kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| C | 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 | 2 |
| Details | binding site for residue CA A 501 |
| Chain | Residue |
| A | ASN207 |
| C | SER423 |
| site_id | AC2 |
| Number of Residues | 20 |
| Details | binding site for residue LRS A 502 |
| Chain | Residue |
| A | VAL263 |
| A | TYR264 |
| A | MET265 |
| A | PRO266 |
| A | GLY268 |
| A | THR280 |
| A | ALA315 |
| A | LEU318 |
| A | HOH606 |
| A | HOH629 |
| A | HOH648 |
| A | HOH655 |
| A | HOH659 |
| A | ILE185 |
| A | MET192 |
| A | GLY193 |
| A | GLU194 |
| A | VAL200 |
| A | ALA211 |
| A | TYR262 |
| site_id | AC3 |
| Number of Residues | 1 |
| Details | binding site for residue CA B 501 |
| Chain | Residue |
| D | ASN207 |
| site_id | AC4 |
| Number of Residues | 14 |
| Details | binding site for residue LRS B 502 |
| Chain | Residue |
| B | MET192 |
| B | ALA211 |
| B | TYR262 |
| B | VAL263 |
| B | TYR264 |
| B | MET265 |
| B | PRO266 |
| B | GLY268 |
| B | THR280 |
| B | ALA315 |
| B | LEU318 |
| B | HOH607 |
| B | HOH608 |
| B | HOH637 |
| site_id | AC5 |
| Number of Residues | 16 |
| Details | binding site for residue LRS C 501 |
| Chain | Residue |
| C | MET192 |
| C | GLU194 |
| C | ALA211 |
| C | TYR262 |
| C | VAL263 |
| C | TYR264 |
| C | MET265 |
| C | PRO266 |
| C | GLY268 |
| C | ASP278 |
| C | ALA315 |
| C | LEU318 |
| C | HOH603 |
| C | HOH605 |
| C | HOH607 |
| C | HOH608 |
| site_id | AC6 |
| Number of Residues | 16 |
| Details | binding site for residue LRS D 501 |
| Chain | Residue |
| D | MET192 |
| D | ALA211 |
| D | TYR262 |
| D | VAL263 |
| D | TYR264 |
| D | MET265 |
| D | PRO266 |
| D | ASN267 |
| D | GLY268 |
| D | THR280 |
| D | ALA315 |
| D | LEU318 |
| D | HOH603 |
| D | HOH605 |
| D | HOH610 |
| D | HOH637 |
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"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 32 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00159","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 20 |
| Details | Binding site: {} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| 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 | 4 |
| 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 | 4 |
| Details | Modified residue: {"description":"Phosphoserine","evidences":[{"source":"PubMed","id":"17161373","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17312103","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
