Research workbench
Crystal structure of a FMN/FAD- and NAD(P)H-dependent nitroreductase (nfnb, IL2077) from idiomarina loihiensis L2TR at 1.90 a resolution
Analyse Crystal structure of a FMN/FAD- and NAD(P)H-dependent nitroreductase (nfnb… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3OF4
- Type
- protein
- Length
- 624 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q5R179
Structure
x-ray diffraction · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C | — | protein | 208 | — | Q5R179 |
Compared structures
- 3OF4 · Crystal structure of a FMN/FAD- and NAD(P)H-dependent nitroreductase (nfnB, IL2077) from… · the same entry in another collection · chain C against C, 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 Q5R179
- Elsewhere: RCSB PDB 3OF4 · PDBe 3OF4 · UniProt Q5R179
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