Research workbench
Structure of pep bound enolase from mycobacterium tuberculosis
Analyse Structure of pep bound enolase from mycobacterium tuberculosis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7E51
- Type
- protein
- Length
- 3,384 residues
- Chains
- 8
- Method
- electron microscopy
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enolase
- EC
- 4.2.1.11
- UniProt
- A0A0E8NV14
- Ligands
- PEP, MG
- Pockets
- 20 · best druggability 0.81
Structure
electron microscopy · 1 distinct chain · 39% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, F, G, H | Enolase (EC 4.2.1.11) | protein | 423 | 39% helix, 19% strand | A0A0E8NV14 |
Ligands and binding sites
- PEP · Phosphoenolpyruvate · ligand · 8 copies · chains A, B, C, D, E, F, G, H
- MG · Magnesium ion · metal · 16 copies · chains A, B, C, D, E, F, G, H
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
20 pockets found on a 1 Å grid, 19 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1002 | 0.81 | 0.82 | 92 | empty |
| 2 | 899 | 0.80 | 0.82 | 79 | empty |
| 3 | 1059 | 0.80 | 0.81 | 110 | empty |
| 4 | 1133 | 0.79 | 0.81 | 113 | empty |
| 5 | 689 | 0.74 | 0.80 | 98 | PEP, MG |
Interfaces
8 interfaces between chains.
- E–F · 1597 Ų buried · 25 hydrogen bonds · protein-protein
- C–D · 1593 Ų buried · 28 hydrogen bonds · protein-protein
- G–H · 1582 Ų buried · 27 hydrogen bonds · protein-protein
- A–B · 1524 Ų buried · 28 hydrogen bonds · protein-protein
- B–C · 1162 Ų buried · 12 hydrogen bonds · protein-protein
Compared structures
- 7E51 · Structure of PEP bound Enolase from Mycobacterium tuberculosis · 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 A0A0E8NV14
- Elsewhere: RCSB PDB 7E51 · PDBe 7E51 · UniProt A0A0E8NV14
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