MolNFT v1 · #25557 · protein
Structure of pentaerythritol tetranitrate reductase W102Y mutant and complexed with picric acid
1VYS: “Structure of pentaerythritol tetranitrate reductase W102Y mutant and complexed with picric acid”. X-ray diffraction, 2 ligands (FMN, TNF), 1 pocket (best druggability 0.76). MolNFT v1 #25557 on GenesisL1: 3D structure, binding sites…
- PDB
- 1VYS
- Type
- protein
- Length
- 364 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Pentaerythritol tetranitrate reductase
- UniProt
- P71278
- Ligands
- FMN, TNF
- Pockets
- 1 · best druggability 0.76
Structure
x-ray diffraction · 1 distinct chain · 34% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| X | Pentaerythritol tetranitrate reductase | protein | 364 | 34% helix, 18% strand | P71278 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 332 | 0.76 | 0.87 | 35 | FMN, TNF |
Compared structures
- 1VYS · Structure of pentaerythritol tetranitrate reductase W102Y mutant and complexed with… · the same entry in another collection · chain X against X, 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 P71278
- Elsewhere: RCSB PDB 1VYS · PDBe 1VYS · UniProt P71278
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