6EGD
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 | 12 |
| Details | binding site for residue J87 D 501 |
| Chain | Residue |
| D | MET192 |
| D | LEU318 |
| D | SER328 |
| D | HOH609 |
| D | ALA211 |
| D | LYS213 |
| D | TYR262 |
| D | VAL263 |
| D | TYR264 |
| D | MET265 |
| D | GLY268 |
| D | ASP272 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | binding site for residue J87 A 501 |
| Chain | Residue |
| A | MET192 |
| A | ALA211 |
| A | LYS213 |
| A | TYR262 |
| A | VAL263 |
| A | TYR264 |
| A | MET265 |
| A | PRO266 |
| A | GLY268 |
| A | LEU318 |
| A | SER328 |
| A | ASP329 |
| A | HOH616 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| D | ASN311 | |
| A | ASN311 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| D | MET192 | |
| A | MET192 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 6 |
| Details | BINDING: |
| Chain | Residue | Details |
| D | LYS213 | |
| D | LYS313 | |
| D | ASP329 | |
| A | LYS213 | |
| A | LYS313 | |
| A | ASP329 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:17312103, ECO:0000269|Ref.32 |
| Chain | Residue | Details |
| D | THR342 | |
| A | THR342 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0000269|PubMed:17161373, ECO:0000269|PubMed:17312103, ECO:0000269|Ref.32 |
| Chain | Residue | Details |
| D | THR345 | |
| A | THR345 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphoserine => ECO:0000269|PubMed:17161373, ECO:0000269|PubMed:17312103 |
| Chain | Residue | Details |
| D | SER346 | |
| A | SER346 |
