Research workbench
Crystal structure of the rwd domain of human GCN2 - 2
Analyse Crystal structure of the rwd domain of human GCN2 - 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E2M
- Type
- protein
- Length
- 775 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Eif-2-alpha kinase GCN2
- EC
- 2.7.11.1
- UniProt
- Q9P2K8
- Pockets
- 5 · best druggability 0.80
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Eif-2-alpha kinase GCN2 (EC 2.7.11.1) | protein | 130 | 38% helix, 19% strand | Q9P2K8 |
| B, C, D, E, F | Eif-2-alpha kinase GCN2 (EC 2.7.11.1) | protein | 129 | 36% helix, 19% strand | Q9P2K8 |
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1136 | 0.80 | 0.81 | 125 | empty |
| 2 | 87 | 0.50 | 0.83 | 22 | empty |
| 3 | 52 | 0.42 | 0.84 | 15 | empty |
| 4 | 81 | 0.42 | 0.80 | 23 | empty |
| 5 | 62 | 0.40 | 0.80 | 16 | empty |
Interfaces
9 interfaces between chains.
- A–B · 1324 Ų buried · 24 hydrogen bonds · protein-protein
- E–F · 1310 Ų buried · 25 hydrogen bonds · protein-protein
- C–D · 1290 Ų buried · 21 hydrogen bonds · protein-protein
- A–E · 268 Ų buried · 5 hydrogen bonds · protein-protein
- A–F · 258 Ų buried · 2 hydrogen bonds · protein-protein
Compared structures
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt Q9P2K8
- Elsewhere: RCSB PDB 7E2M · PDBe 7E2M · UniProt Q9P2K8
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