Research workbench
Crystal structure of ef-G-2 from thermus thermophilus
Analyse Crystal structure of ef-G-2 from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2DY1
- Type
- protein
- Length
- 660 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor G
- UniProt
- Q5SI76
- Ligands
- GTP, MG
- Pockets
- 6 · best druggability 0.57
Structure
x-ray diffraction · 1 distinct chain · 33% helix, 34% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor G | protein | 660 | 33% helix, 34% strand | Q5SI76 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 169 | 0.57 | 0.81 | 29 | empty |
| 2 | 182 | 0.56 | 0.80 | 28 | empty |
| 3 | 239 | 0.51 | 0.75 | 34 | empty |
| 4 | 141 | 0.50 | 0.79 | 25 | MG, GTP |
| 5 | 65 | 0.33 | 0.75 | 17 | empty |
Compared structures
- 2DY1 · Crystal structure of EF-G-2 from Thermus thermophilus · the same entry in another collection · chain A against A, TM-score 1.00
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 Q5SI76
- Elsewhere: RCSB PDB 2DY1 · PDBe 2DY1 · UniProt Q5SI76
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