Research workbench
L-3-hydroxyacyl-CoA dehydrogenase complexed with 3-hydroxybutyryl-CoA
Analyse L-3-hydroxyacyl-CoA dehydrogenase complexed with 3-hydroxybutyryl-CoA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1F12
- Type
- protein
- Length
- 584 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- L-3-hydroxyacyl-CoA dehydrogenase
- EC
- 1.1.1.35
- UniProt
- Q16836
- Ligands
- 3HC
- Pockets
- 11 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | L-3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) | protein | 293 | 52% helix, 14% strand | Q16836 |
| B | L-3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) | protein | 291 | 51% helix, 14% strand | Q16836 |
Ligands and binding sites
- 3HC · 3-hydroxybutanoyl-coenzyme A · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
11 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 452 | 0.71 | 0.81 | 47 | empty |
| 2 | 423 | 0.67 | 0.79 | 45 | empty |
| 3 | 71 | 0.45 | 0.82 | 21 | empty |
| 4 | 106 | 0.39 | 0.75 | 20 | empty |
| 5 | 101 | 0.38 | 0.75 | 22 | empty |
Interfaces
1 interface between chains.
- A–B · 1680 Ų buried · 5 hydrogen bonds · protein-protein
Compared structures
- 1F12 · L-3-hydroxyacyl-CoA dehydrogenase complexed with 3-hydroxybutyryl-CoA · the same entry in another collection · chain A against A, TM-score 1.00
- Q16836 · AlphaFold monomer V2.0 prediction for hydroxyacyl-coenzyme a dehydrogenase, mitochondrial… · 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 Q16836
- Elsewhere: RCSB PDB 1F12 · PDBe 1F12 · UniProt Q16836
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