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The major NAD(P)H:FMN oxidoreductase from vibrio fischeri

Analyse The major NAD(P)H:FMN oxidoreductase from vibrio fischeri in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1VFR
Type
protein
Length
434 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
NAD(P)H\:FMN oxidoreductase
EC
1.6.99.-
UniProt
P46072
Ligands
FMN
Pockets
3 · best druggability 0.75

Structure

x-ray diffraction · 1 distinct chain · 49% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BNAD(P)H\:FMN oxidoreductase (EC 1.6.99.-)protein21749% helix, 16% strandP46072

Ligands and binding sites

  • FMN · Flavin mononucleotide · ligand · 2 copies · chains A, B

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

3 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14640.750.8445FMN
24800.750.8447FMN
33270.570.7641empty

Interfaces

1 interface between chains.

  • A–B · 3545 Ų buried · 58 hydrogen bonds · protein-protein

Compared structures

  • 1VFR · The major NAD(P)H:FMN oxidoreductase from vibrio fischeri · the same entry in another collection · chain A against A, TM-score 1.00
  • P46072 · AlphaFold monomer V2.0 prediction for major NAD(P)H-flavin oxidoreductase (P46072) · a predicted model of the same protein · chain A against A, TM-score 0.99

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