Research workbench
NADPH:FMN oxidoreductase from vibrio harveyi complexed with NAD+
Analyse NADPH:FMN oxidoreductase from vibrio harveyi complexed with NAD+ in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2BKJ
- Type
- protein
- Length
- 460 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Flavin reductase
- EC
- 1.6.99.-
- UniProt
- Q56691
- Ligands
- FMN, NAD
- Pockets
- 2 · best druggability 0.63
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Flavin reductase (EC 1.6.99.-) | protein | 230 | 49% helix, 14% strand | Q56691 |
Ligands and binding sites
- FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B
- NAD · Nicotinamide-adenine-dinucleotide · ligand · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 295 | 0.63 | 0.80 | 47 | FMN |
| 2 | 268 | 0.62 | 0.80 | 39 | FMN |
Interfaces
1 interface between chains.
- A–B · 4603 Ų buried · 64 hydrogen bonds · protein-protein
Compared structures
- 2BKJ · NADPH:FMN oxidoreductase from vibrio harveyi complexed with NAD+ · the same entry in another collection · chain A against A, TM-score 1.00
- Q56691 · AlphaFold monomer V2.0 prediction for NADPH-flavin oxidoreductase (Q56691) · a predicted model of the same protein · chain B 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 Q56691
- Elsewhere: RCSB PDB 2BKJ · PDBe 2BKJ · UniProt Q56691
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