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X-ray structure of FAD domain of nqrf of klebsiella pneumoniae

Analyse X-ray structure of FAD domain of nqrf of klebsiella pneumoniae in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
7QTY
Type
protein
Length
279 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Na(+)-translocating NADH-quinone reductase subunit F
EC
7.2.1.1
UniProt
A6T526
Ligands
FAD, F0R
Pockets
1 · best druggability 0.65

Structure

x-ray diffraction · 1 distinct chain · 30% helix, 31% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
ANa(+)-translocating NADH-quinone reductase subunit F (EC 7.2.1.1)protein27930% helix, 31% strandA6T526

Ligands and binding sites

  • FAD · Flavin-adenine dinucleotide · ligand · chains A
  • F0R · 1-(furan-2-ylmethyl)-3-(2-methylphenyl)thiourea · ligand · chains A
  • DMS · Dimethyl sulfoxide · additive · 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, 1 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
15050.650.7761FAD, F0R

Compared structures

  • 7QTY · X-ray structure of FAD domain of NqrF of Klebsiella pneumoniae · the same entry in another collection · chain A against A, TM-score 1.00
  • A6T526 · AlphaFold monomer V2.0 prediction for na(+)-translocating NADH- quinone reductase subunit… · a predicted model of the same protein · chain A against A, TM-score 0.99

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