Research workbench
Crystal structure of 2-enoyl thioester reductase of human fas II
Analyse Crystal structure of 2-enoyl thioester reductase of human fas II in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2VCY
- Type
- protein
- Length
- 664 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Trans-2-enoyl-CoA reductase
- EC
- 1.3.1.38
- UniProt
- Q9BV79
- Ligands
- SO4
- Pockets
- 8 · best druggability 0.80
Structure
x-ray diffraction · 1 distinct chain · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Trans-2-enoyl-CoA reductase (EC 1.3.1.38) | protein | 332 | 31% helix, 25% strand | Q9BV79 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 11 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 819 | 0.80 | 0.83 | 79 | SO4 |
| 2 | 709 | 0.77 | 0.82 | 62 | SO4 |
| 3 | 53 | 0.50 | 0.86 | 13 | empty |
| 4 | 74 | 0.49 | 0.83 | 15 | empty |
| 5 | 73 | 0.37 | 0.78 | 14 | empty |
Interfaces
1 interface between chains.
- A–B · 1125 Ų buried · 10 hydrogen bonds · protein-protein
Compared structures
- 2VCY · Crystal Structure of 2-Enoyl Thioester Reductase of Human FAS II · the same entry in another collection · chain A against A, TM-score 1.00
- Q9BV79 · AlphaFold monomer V2.0 prediction for enoyl-[acyl-carrier-protein] reductase… · a predicted model of the same protein · chain A 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 Q9BV79
- Elsewhere: RCSB PDB 2VCY · PDBe 2VCY · UniProt Q9BV79
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