Research workbench
Gluconobacter ene-reductase (gluer)
Analyse Gluconobacter ene-reductase (gluer) in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6O08
- Type
- protein
- Length
- 360 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-ethylmaleimide reductase
- UniProt
- A1E8I9
- Ligands
- FMN, NA, SO4, CL
- Pockets
- 1 · best druggability 0.74
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-ethylmaleimide reductase | protein | 360 | 34% helix, 16% strand | A1E8I9 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains A
- NA · Sodium ion · metal · chains A
- SO4 · Sulfate ion · ion · 4 copies · chains A
- CL · Chloride ion · ion · 2 copies · chains A
- ACT · Acetate ion · additive · 5 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 357 | 0.74 | 0.85 | 52 | FMN, ACT, NA |
Compared structures
- 6O08 · Gluconobacter Ene-Reductase (GluER) · 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 A1E8I9
- Elsewhere: RCSB PDB 6O08 · PDBe 6O08 · UniProt A1E8I9
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