Research workbench
Crystal structure of the N208S mutant of L-3-hydroxyacyl-CoA dehydrogenase in complex with NAD and acetoacetyl-CoA
Analyse Crystal structure of the N208S mutant of L-3-hydroxyacyl-CoA dehydrogenase in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1M75
- Type
- protein
- Length
- 582 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 3-hydroxyacyl-CoA dehydrogenase
- EC
- 1.1.1.35
- UniProt
- Q16836
- Ligands
- CAA, NAD
- Pockets
- 5 · best druggability 0.75
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35) | protein | 291 | 48% helix, 14% strand | Q16836 |
Ligands and binding sites
- CAA · Acetoacetyl-coenzyme A · ligand · 2 copies · chains A, B
- NAD · Nicotinamide-adenine-dinucleotide · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 684 | 0.75 | 0.81 | 74 | CAA, NAD |
| 2 | 704 | 0.75 | 0.80 | 74 | CAA, NAD |
| 3 | 154 | 0.52 | 0.79 | 34 | empty |
| 4 | 58 | 0.32 | 0.76 | 14 | empty |
| 5 | 50 | 0.28 | 0.75 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1635 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 1M75 · Crystal Structure of the N208S Mutant of L-3-Hydroxyacyl-COA Dehydrogenase in Complex… · 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 A against A, TM-score 0.92
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 1M75 · PDBe 1M75 · UniProt Q16836
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