Research workbench
Crystal structure of the nitroreductase-like family protein from bacillus cereus
Analyse Crystal structure of the nitroreductase-like family protein from bacillus cereus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2I7H
- Type
- protein
- Length
- 1,120 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nitroreductase-like family protein
- UniProt
- Q81HL8
- Ligands
- FMN, SO4
- Pockets
- 16 · best druggability 0.68
Structure
x-ray diffraction · 2 distinct chains · 47% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D, F | Nitroreductase-like family protein | protein | 187 | 47% helix, 21% strand | Q81HL8 |
| E | Nitroreductase-like family protein | protein | 185 | 48% helix, 18% strand | Q81HL8 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 4 copies · chains A, B, C, D
- SO4 · Sulfate ion · ion · 7 copies · chains A, B, C, D, E, F
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
16 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 181 | 0.68 | 0.87 | 32 | FMN |
| 2 | 283 | 0.67 | 0.83 | 46 | FMN |
| 3 | 265 | 0.67 | 0.83 | 43 | SO4 |
| 4 | 254 | 0.66 | 0.83 | 45 | SO4, FMN |
| 5 | 221 | 0.65 | 0.84 | 34 | empty |
Interfaces
6 interfaces between chains.
- A–B · 3411 Ų buried · 54 hydrogen bonds · protein-protein
- C–D · 3406 Ų buried · 54 hydrogen bonds · protein-protein
- E–F · 3388 Ų buried · 48 hydrogen bonds · protein-protein
- B–C · 528 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 312 Ų buried · 5 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 24 modified (engineered).
Compared structures
- 2I7H · Crystal Structure of the Nitroreductase-like Family Protein from Bacillus cereus · the same entry in another collection · chain A against A, 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 Q81HL8
- Elsewhere: RCSB PDB 2I7H · PDBe 2I7H · UniProt Q81HL8
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.