MolNFT v2 · #210766 · protein
Structure of PmHMGR bound to mevalonate, CoA and NAD.
8GDN: “Structure of PmHMGR bound to mevalonate, CoA and NAD.”. X-ray diffraction at 1.99, 4 ligands (MEV, COA, NAD). MolNFT v2 #210766 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 8GDN
- Type
- protein
- Length
- 799 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.99
- Source
- Pseudomonas sp. 'mevalonii'
- UniProt
- P13702
- Ligands
- MEV, COA, NAD, SO4
Structure
x-ray diffraction · resolution 1.99 · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 421 | — | P13702 |
| B | — | protein | 378 | — | P13702 |
Ligands and binding sites
- MEV · (R)-mevalonate · ligand · 2 copies · chains A, B
- COA · Coenzyme A · ligand · chains A, B
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A, B
- SO4 · Sulfate ion · ion · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- P13702 · AlphaFold monomer V2.0 prediction for 3-hydroxy-3-methylglutaryl- coenzyme a reductase… · a predicted model of the same protein · chain B against A, TM-score 0.99
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 P13702
- Elsewhere: RCSB PDB 8GDN · PDBe 8GDN · UniProt P13702
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