7QWK
GCN2 (EIF2ALPHA KINASE 4, E2AK4) IN COMPLEX WITH COMPOUND 2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004672 | molecular_function | protein kinase activity |
| A | 0005524 | molecular_function | ATP binding |
| A | 0006468 | biological_process | protein phosphorylation |
| B | 0004672 | molecular_function | protein kinase activity |
| B | 0005524 | molecular_function | ATP binding |
| B | 0006468 | biological_process | protein phosphorylation |
| C | 0004672 | molecular_function | protein kinase activity |
| C | 0005524 | molecular_function | ATP binding |
| C | 0006468 | biological_process | protein phosphorylation |
| D | 0004672 | molecular_function | protein kinase activity |
| D | 0005524 | molecular_function | ATP binding |
| D | 0006468 | biological_process | protein phosphorylation |
| E | 0004672 | molecular_function | protein kinase activity |
| E | 0005524 | molecular_function | ATP binding |
| E | 0006468 | biological_process | protein phosphorylation |
| F | 0004672 | molecular_function | protein kinase activity |
| F | 0005524 | molecular_function | ATP binding |
| F | 0006468 | biological_process | protein phosphorylation |
| G | 0004672 | molecular_function | protein kinase activity |
| G | 0005524 | molecular_function | ATP binding |
| G | 0006468 | biological_process | protein phosphorylation |
| H | 0004672 | molecular_function | protein kinase activity |
| H | 0005524 | molecular_function | ATP binding |
| H | 0006468 | biological_process | protein phosphorylation |
Functional Information from PROSITE/UniProt
| site_id | PS00107 |
| Number of Residues | 24 |
| Details | PROTEIN_KINASE_ATP Protein kinases ATP-binding region signature. LGKGAFGAVIkVqnkldgcc..........YAVK |
| Chain | Residue | Details |
| A | LEU596-LYS619 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00159, ECO:0000255|PROSITE-ProRule:PRU10027 |
| Chain | Residue | Details |
| A | GLN974 | |
| B | GLN974 | |
| C | GLN974 | |
| D | GLN974 | |
| E | GLN974 | |
| F | GLN974 | |
| G | GLN974 | |
| H | GLN974 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 16 |
| Details | BINDING: BINDING => ECO:0000255|PROSITE-ProRule:PRU00159 |
| Chain | Residue | Details |
| A | LEU596 | |
| A | LYS619 | |
| B | LEU596 | |
| B | LYS619 | |
| C | LEU596 | |
| C | LYS619 | |
| D | LEU596 | |
| D | LYS619 | |
| E | LEU596 | |
| E | LYS619 | |
| F | LEU596 | |
| F | LYS619 | |
| G | LEU596 | |
| G | LYS619 | |
| H | LEU596 | |
| H | LYS619 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19369195, ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| G | GLU793 | |
| H | GLU793 | |
| A | GLU793 | |
| B | GLU793 | |
| C | GLU793 | |
| D | GLU793 | |
| E | GLU793 | |
| F | GLU793 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:23186163 |
| Chain | Residue | Details |
| A | LYS997 | |
| B | LYS997 | |
| C | LYS997 | |
| D | LYS997 | |
| E | LYS997 | |
| F | LYS997 | |
| G | LYS997 | |
| H | LYS997 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250|UniProtKB:Q9QZ05 |
| Chain | Residue | Details |
| site_id | SWS_FT_FI6 |
| Number of Residues | 8 |
| Details | MOD_RES: Phosphothreonine; by autocatalysis => ECO:0000250 |
| Chain | Residue | Details |
