MolNFT v1 · #175029 · protein
Crystal structure of mycobacterium tuberculosis elongation factor G1
7CDW: “Crystal structure of mycobacterium tuberculosis elongation factor G1”. X-ray diffraction, 1 ligand (GDP), 20 pockets (best druggability 0.81). MolNFT v1 #175029 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 7CDW
- Type
- protein
- Length
- 1,361 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongation factor G
- UniProt
- P9WNM7
- Ligands
- GDP
- Pockets
- 20 · best druggability 0.81
Structure
x-ray diffraction · 2 distinct chains · 29% helix, 33% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongation factor G | protein | 683 | 30% helix, 33% strand | P9WNM7 |
| B | Elongation factor G | protein | 678 | 27% helix, 34% strand | P9WNM7 |
Ligands and binding sites
- GDP · Guanosine-5'-diphosphate · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 11 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 886 | 0.81 | 0.83 | 80 | GDP |
| 2 | 779 | 0.78 | 0.82 | 78 | empty |
| 3 | 605 | 0.75 | 0.82 | 57 | empty |
| 4 | 190 | 0.61 | 0.82 | 24 | empty |
| 5 | 170 | 0.60 | 0.83 | 26 | empty |
Interfaces
1 interface between chains.
- A–B · 1980 Ų buried · 17 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 32 modified (engineered).
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 P9WNM7
- Elsewhere: RCSB PDB 7CDW · PDBe 7CDW · UniProt P9WNM7
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