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 |