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Crystal structure of elongation factor 2
Analyse Crystal structure of elongation factor 2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1N0V
- Type
- protein
- Length
- 1,650 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor 2
- UniProt
- P32324
- Pockets
- 17 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C, D | Elongation factor 2 | protein | 825 | 37% helix, 26% strand | P32324 |
Pockets
17 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 993 | 0.81 | 0.82 | 99 | empty |
| 2 | 630 | 0.78 | 0.83 | 56 | empty |
| 3 | 743 | 0.67 | 0.75 | 76 | empty |
| 4 | 474 | 0.62 | 0.76 | 53 | empty |
| 5 | 211 | 0.51 | 0.76 | 20 | empty |
Interfaces
1 interface between chains.
- C–D · 184 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 P32324
- Elsewhere: RCSB PDB 1N0V · PDBe 1N0V · UniProt P32324
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