Research workbench
Translational elongation factor G complexed with GDP
Analyse Translational elongation factor G complexed with GDP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2EFG
- Type
- protein
- Length
- 634 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Protein (elongation factor G); Protein (elongation factor G domain 3)
- UniProt
- P13551
- Ligands
- GDP
- Pockets
- 4 · best druggability 0.74
Structure
x-ray diffraction · 2 distinct chains · 28% helix, 30% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Protein (elongation factor G) | protein | 582 | 27% helix, 33% strand | P13551 |
| B | Protein (elongation factor G domain 3) | protein | 52 | 31% helix, 4% strand | — |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1140 | 0.74 | 0.77 | 97 | empty |
| 2 | 213 | 0.61 | 0.82 | 36 | empty |
| 3 | 198 | 0.58 | 0.81 | 28 | empty |
| 4 | 52 | 0.27 | 0.74 | 13 | empty |
Interfaces
1 interface between chains.
- A–B · 569 Ų buried · 4 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 P13551
- Elsewhere: RCSB PDB 2EFG · PDBe 2EFG · UniProt P13551
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