Research workbench
Crystal structure of enolase from legionella pneumophila bound to phosphate and magnesium
Analyse Crystal structure of enolase from legionella pneumophila bound to phosphate and… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NBM
- Type
- protein
- Length
- 847 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Enolase
- EC
- 4.2.1.11
- UniProt
- A0A2S6F4U1
- Ligands
- MG, PO4
- Pockets
- 6 · best druggability 0.75
Structure
x-ray diffraction · 2 distinct chains · 43% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Enolase (EC 4.2.1.11) | protein | 423 | 43% helix, 19% strand | A0A2S6F4U1 |
| B | Enolase (EC 4.2.1.11) | protein | 424 | 43% helix, 19% strand | A0A2S6F4U1 |
Ligands and binding sites
- MG · Magnesium ion · metal · 4 copies · chains A, B
- PO4 · Phosphate ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
6 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1179 | 0.75 | 0.78 | 60 | empty |
| 2 | 132 | 0.50 | 0.80 | 32 | empty |
| 3 | 148 | 0.50 | 0.79 | 29 | empty |
| 4 | 68 | 0.36 | 0.77 | 18 | empty |
| 5 | 73 | 0.35 | 0.76 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 1794 Ų buried · 47 hydrogen bonds · protein-protein
Compared structures
- 6NBM · Crystal structure of enolase from legionella pneumophila bound to phosphate and magnesium · 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 A0A2S6F4U1
- Elsewhere: RCSB PDB 6NBM · PDBe 6NBM · UniProt A0A2S6F4U1
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