Research workbench
2.60 ångström resolution crystal structure of elongation factor G 2 from pseudomonas putida.
Analyse 2.60 ångström resolution crystal structure of elongation factor G 2 from… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6N0I
- Type
- protein
- Length
- 1,353 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor G 2
- UniProt
- Q88FI4
- Ligands
- SO4
- Pockets
- 20 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor G 2 | protein | 674 | 30% helix, 33% strand | Q88FI4 |
| B | Elongation factor G 2 | protein | 679 | 30% helix, 33% strand | Q88FI4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 15 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 653 | 0.79 | 0.84 | 82 | empty |
| 2 | 633 | 0.76 | 0.82 | 48 | empty |
| 3 | 64 | 0.73 | 0.98 | 27 | empty |
| 4 | 497 | 0.72 | 0.82 | 53 | empty |
| 5 | 252 | 0.65 | 0.83 | 38 | empty |
Interfaces
1 interface between chains.
- A–B · 1691 Ų buried · 21 hydrogen bonds · protein-protein
Compared structures
- 6N0I · 2.60 Angstrom Resolution Crystal Structure of Elongation Factor G 2 from Pseudomonas… · the same entry in another collection · chain A against A, TM-score 1.00
- Q88FI4 · AlphaFold monomer V2.0 prediction for elongation factor G 2 (Q88FI4) · a predicted model of the same protein · chain A against A, TM-score 0.73
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 Q88FI4
- Elsewhere: RCSB PDB 6N0I · PDBe 6N0I · UniProt Q88FI4
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