Research workbench
NADH oxidase from thermus thermophilus
Analyse NADH oxidase from thermus thermophilus in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NOX
- Type
- protein
- Length
- 200 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NADH oxidase
- EC
- 1.6.99.3
- UniProt
- Q60049
- Ligands
- FMN
Structure
x-ray diffraction · 1 distinct chain · 48% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NADH oxidase (EC 1.6.99.3) | protein | 200 | 48% helix, 15% strand | Q60049 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 Q60049
- Elsewhere: RCSB PDB 1NOX · PDBe 1NOX · UniProt Q60049
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