Research workbench
Structure of an integral membrane DELTA(14)-sterol reductase
Analyse Structure of an integral membrane DELTA(14)-sterol reductase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QUV
- Type
- protein
- Length
- 782 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DELTA(14)-sterol reductase
- EC
- 1.3.1.70
- UniProt
- G4SW86
- Ligands
- NDP
- Pockets
- 5 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 66% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DELTA(14)-sterol reductase (EC 1.3.1.70) | protein | 393 | 67% helix, 6% strand | G4SW86 |
| B | DELTA(14)-sterol reductase (EC 1.3.1.70) | protein | 389 | 65% helix, 6% strand | G4SW86 |
Ligands and binding sites
- NDP · Nadph dihydro-nicotinamide-adenine-dinucleotide phosphate · 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 | 1079 | 0.83 | 0.83 | 97 | empty |
| 2 | 842 | 0.83 | 0.85 | 69 | NDP |
| 3 | 936 | 0.82 | 0.83 | 69 | NDP |
| 4 | 87 | 0.49 | 0.82 | 21 | empty |
| 5 | 59 | 0.30 | 0.73 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 737 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
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 G4SW86
- Elsewhere: RCSB PDB 4QUV · PDBe 4QUV · UniProt G4SW86
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