Research workbench
E. COLI nfsa with 1,4-benzoquinone
Analyse E. COLI nfsa with 1,4-benzoquinone in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7NNX
- Type
- protein
- Length
- 240 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Oxygen-insensitive NADPH nitroreductase
- EC
- 1.-.-.-
- UniProt
- P17117
- Ligands
- HQE, FMN, PLQ, CL
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Oxygen-insensitive NADPH nitroreductase (EC 1.-.-.-) | protein | 240 | 48% helix, 13% strand | P17117 |
Ligands and binding sites
- HQE · benzene-1,4-diol · ligand · chains A
- FMN · Flavin mononucleotide · ligand · chains A
- PLQ · 1,4-benzoquinone · ligand · chains A
- CL · Chloride ion · ion · chains A
- EDO · 1,2-ethanediol · additive · 3 copies · chains A
- DMS · Dimethyl sulfoxide · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Modifications
Observed in the structure: 1 covalent (covalent ligand).
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 P17117
- Elsewhere: RCSB PDB 7NNX · PDBe 7NNX · UniProt P17117
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