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Crystal structure of NAD(P)H-flavin oxidoreductase from helicobacter pylori

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

PDB
2H0U
Type
protein
Length
196 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
NADPH-flavin oxidoreductase
UniProt
Q7BGI8
Ligands
FMN

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 16% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANADPH-flavin oxidoreductaseprotein19644% helix, 16% strandQ7BGI8

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.

Modifications

Observed in the structure: 9 modified (engineered).

Compared structures

  • 2H0U · Crystal structure of NAD(P)H-flavin oxidoreductase from Helicobacter pylori · the same entry in another collection · chain A against A, TM-score 1.00

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