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Crystal structure of NAD(P)H:FLAVIN oxidoreductase from escherichia COLI

Analyse Crystal structure of NAD(P)H:FLAVIN oxidoreductase from escherichia COLI in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1QFJ
Type
protein
Length
904 residues
Chains
4
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (flavin reductase)
UniProt
P23486
Pockets
9 · best druggability 0.72

Structure

x-ray diffraction · 1 distinct chain · 29% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, DProtein (flavin reductase)protein22629% helix, 31% strandP23486

Ligands and binding sites

  • GOL · Glycerol · additive · 4 copies · chains A, B, C, D

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

Pockets

9 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
19570.720.7672empty
24290.700.8152GOL
34190.690.8048GOL
43190.670.8248GOL
51420.610.8528empty

Interfaces

3 interfaces between chains.

  • A–B · 949 Ų buried · 14 hydrogen bonds · protein-protein
  • C–D · 920 Ų buried · 14 hydrogen bonds · protein-protein
  • A–D · 334 Ų buried · 1 hydrogen bond · protein-protein

Compared structures

  • 1QFJ · Crystal structure of NAD(P)H:FLAVIN oxidoreductase from escherichia COLI · the same entry in another collection · chain A against A, TM-score 1.00

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