Research workbench
Structure of NFRA1 nitroreductase from B. subtilis
Analyse Structure of NFRA1 nitroreductase from B. subtilis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3N2S
- Type
- protein
- Length
- 991 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADPH-dependent NITRO/FLAVIN reductase
- EC
- 1.5.1.29
- UniProt
- P39605
- Ligands
- FMN, CL
- Pockets
- 8 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 52% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | NADPH-dependent NITRO/FLAVIN reductase (EC 1.5.1.29) | protein | 248 | 52% helix, 14% strand | P39605 |
| D | NADPH-dependent NITRO/FLAVIN reductase (EC 1.5.1.29) | protein | 247 | 52% helix, 14% strand | P39605 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 4 copies · chains A, B, C, D
- CL · Chloride ion · ion · 2 copies · chains A, C, 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, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1177 | 0.86 | 0.87 | 146 | FMN, CL |
| 2 | 346 | 0.70 | 0.83 | 47 | FMN |
| 3 | 377 | 0.64 | 0.79 | 42 | FMN, CL |
| 4 | 58 | 0.55 | 0.89 | 17 | empty |
| 5 | 50 | 0.36 | 0.80 | 11 | empty |
Interfaces
4 interfaces between chains.
- C–D · 5307 Ų buried · 80 hydrogen bonds · protein-protein
- A–B · 5211 Ų buried · 84 hydrogen bonds · protein-protein
- A–C · 1056 Ų buried · 18 hydrogen bonds · protein-protein
- B–C · 94 Ų buried · 2 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
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 P39605
- Elsewhere: RCSB PDB 3N2S · PDBe 3N2S · UniProt P39605
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.