Research workbench
Crystal structure of FMN-dependent azoreductase from enterococcus faecalis
Analyse Crystal structure of FMN-dependent azoreductase from enterococcus faecalis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HPV
- Type
- protein
- Length
- 828 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q831B2
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | — | protein | 207 | — | Q831B2 |
Compared structures
- 2HPV · Crystal structure of FMN-Dependent azoreductase from Enterococcus faecalis · the same entry in another collection · chain D against D, TM-score 1.00
- Q831B2 · AlphaFold monomer V2.0 prediction for FMN-dependent NADH:QUINONE oxidoreductase (Q831B2) · a predicted model of the same protein · chain D against A, TM-score 0.99
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 Q831B2
- Elsewhere: RCSB PDB 2HPV · PDBe 2HPV · UniProt Q831B2
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