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Fera - NADH:FMN oxidoreductase from paracoccus denitrificans in complex with FMN

Analyse Fera - NADH:FMN oxidoreductase from paracoccus denitrificans in complex with FMN in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
4XJ2
Type
protein
Length
162 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Flavin reductase domain protein, FMN-binding protein
UniProt
A1B5I2
Ligands
FMN
Pockets
1 · best druggability 0.39

Structure

x-ray diffraction · 1 distinct chain · 12% helix, 43% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AFlavin reductase domain protein, FMN-binding proteinprotein16212% helix, 43% strandA1B5I2

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.

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11260.390.7421FMN

Compared structures

  • 4XJ2 · FerA - NADH:FMN oxidoreductase from Paracoccus denitrificans in complex with FMN · the same entry in another collection · chain A against A, TM-score 1.00

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