Research workbench
Crystal structure of an enolase from alpha pretobacterium bal199 (EFI TARGET EFI-501650) with bound MG
Analyse Crystal structure of an enolase from alpha pretobacterium bal199 (EFI TARGET… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3UGV
- Type
- protein
- Length
- 2,905 residues
- Chains
- 8
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.3
- Source
- alpha proteobacterium BAL199
- Molecule
- Enolase
- UniProt
- A8TYI5
- Ligands
- MG, NI, CL
- Pockets
- 20 · best druggability 0.86
Structure
x-ray diffraction · resolution 2.3 · 2 distinct chains · 41% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, E, G, H | Enolase | protein | 363 | 41% helix, 22% strand | A8TYI5 |
| F | Enolase | protein | 364 | 41% helix, 22% strand | A8TYI5 |
Ligands and binding sites
- MG · Magnesium ion · metal · 16 copies · chains A, D, B, C, E, H, F, G
- NI · Nickel (II) ion · metal · 2 copies · chains A, B, C, D, E, F, G, H
- CL · Chloride ion · ion · 3 copies · chains A, G, B, F, D, 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, 20 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1001 | 0.86 | 0.86 | 117 | MG |
| 2 | 802 | 0.84 | 0.87 | 100 | empty |
| 3 | 179 | 0.80 | 0.95 | 28 | empty |
| 4 | 184 | 0.80 | 0.95 | 27 | empty |
| 5 | 172 | 0.80 | 0.95 | 26 | empty |
Interfaces
20 interfaces between chains.
- D–G · 1668 Ų buried · 25 hydrogen bonds · protein-protein
- C–H · 1667 Ų buried · 23 hydrogen bonds · protein-protein
- B–E · 1657 Ų buried · 22 hydrogen bonds · protein-protein
- A–F · 1615 Ų buried · 23 hydrogen bonds · protein-protein
- B–F · 1169 Ų buried · 19 hydrogen bonds · protein-protein
Compared structures
- 3UGV · Crystal structure of an enolase from alpha pretobacterium BAL199 (efi target efi-501650)… · 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 A8TYI5
- Elsewhere: RCSB PDB 3UGV · PDBe 3UGV · UniProt A8TYI5
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