MolNFT v1 · #147496 · protein
Structure of class II hmg-CoA reductase from delftia acidovorans with mevalonate bound
6EEV: “Structure of class II hmg-CoA reductase from delftia acidovorans with mevalonate bound”. X-ray diffraction, 4 ligands (MEV, GLC, FRU). MolNFT v1 #147496 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 6EEV
- Type
- protein
- Length
- 374 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A9BQX8
- Ligands
- MEV, GLC, FRU, SO4
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 374 | — | A9BQX8 |
Ligands and binding sites
- MEV · (R)-mevalonate · ligand · chains A
- GLC · alpha-D-glucopyranose · sugar · 2 copies · chains A
- FRU · beta-D-fructofuranose · sugar · 2 copies · chains A
- SO4 · Sulfate ion · ion · 3 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 6EEV · Structure of class II HMG-CoA reductase from Delftia acidovorans with mevalonate bound · 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 A9BQX8
- Elsewhere: RCSB PDB 6EEV · PDBe 6EEV · UniProt A9BQX8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.