6O95
Structure of the IRAK4 kinase domain with compound 41
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 | 6 |
| Details | binding site for residue SO4 A 501 |
| Chain | Residue |
| A | ASP422 |
| A | SER423 |
| A | HOH622 |
| B | LYS174 |
| B | ASN179 |
| C | ASN207 |
| site_id | AC2 |
| Number of Residues | 11 |
| Details | binding site for residue LSV A 502 |
| Chain | Residue |
| A | VAL263 |
| A | MET265 |
| A | PRO266 |
| A | GLY268 |
| A | LEU318 |
| A | HOH606 |
| A | HOH636 |
| A | HOH723 |
| A | MET192 |
| A | ALA211 |
| A | TYR262 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | binding site for residue LSV B 501 |
| Chain | Residue |
| B | ALA211 |
| B | TYR262 |
| B | VAL263 |
| B | MET265 |
| B | PRO266 |
| B | GLY268 |
| B | LEU318 |
| B | HOH640 |
| site_id | AC4 |
| Number of Residues | 15 |
| Details | binding site for residue LSV C 501 |
| Chain | Residue |
| C | ILE185 |
| C | MET192 |
| C | GLY193 |
| C | VAL200 |
| C | ALA211 |
| C | TYR262 |
| C | VAL263 |
| C | MET265 |
| C | PRO266 |
| C | GLY268 |
| C | ALA315 |
| C | LEU318 |
| C | HOH604 |
| C | HOH660 |
| C | HOH722 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | binding site for residue SO4 D 501 |
| Chain | Residue |
| B | ASN207 |
| D | ASP422 |
| D | SER423 |
| D | HOH662 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | binding site for residue SO4 D 502 |
| Chain | Residue |
| D | GLY350 |
| D | THR351 |
| D | THR352 |
| D | HOH660 |
| D | HOH719 |
| D | HOH762 |
| site_id | AC7 |
| Number of Residues | 12 |
| Details | binding site for residue LSV D 503 |
| Chain | Residue |
| D | MET192 |
| D | GLY193 |
| D | ALA211 |
| D | TYR262 |
| D | VAL263 |
| D | MET265 |
| D | PRO266 |
| D | GLY268 |
| D | LEU318 |
| D | HOH601 |
| D | HOH605 |
| D | HOH739 |
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 | 3 |
| 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 |
