7QG2
IRAK4 in complex with 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 |
| 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 SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | GLN435 | |
| B | GLN435 | |
| C | GLN435 | |
| D | GLN435 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | ASN316 | |
| B | ASN316 | |
| C | ASN316 | |
| D | ASN316 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: |
| Chain | Residue | Details |
| B | LEU437 | |
| B | LEU453 | |
| C | GLU337 | |
| C | LEU437 | |
| C | LEU453 | |
| D | GLU337 | |
| D | LEU437 | |
| D | LEU453 | |
| A | GLU337 | |
| A | LEU437 | |
| A | LEU453 | |
| B | GLU337 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-acetyllysine => ECO:0007744|PubMed:19608861 |
| Chain | Residue | Details |
| A | LEU158 | |
| B | LEU158 | |
| C | LEU158 | |
| D | LEU158 |
