Research workbench
Structure of hmg-CoA reductase from burkholderia cenocepacia
Analyse Structure of hmg-CoA reductase from burkholderia cenocepacia in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6P7K
- Type
- protein
- Length
- 375 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-hydroxy-3-methylglutaryl coenzyme a reductase
- EC
- 1.1.1.88
- UniProt
- A0A2X1DZS9
- Ligands
- ADP, COA
- Pockets
- 3 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | 3-hydroxy-3-methylglutaryl coenzyme a reductase (EC 1.1.1.88) | protein | 375 | 48% helix, 20% strand | A0A2X1DZS9 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 655 | 0.69 | 0.77 | 77 | empty |
| 2 | 67 | 0.32 | 0.75 | 22 | empty |
| 3 | 51 | 0.28 | 0.74 | 14 | empty |
Compared structures
- 6P7K · Structure of HMG-CoA reductase from Burkholderia cenocepacia · 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 A0A2X1DZS9
- Elsewhere: RCSB PDB 6P7K · PDBe 6P7K · UniProt A0A2X1DZS9
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