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Structural basis of multidrug transport by the acrb multidrug efflux pump

Analyse Structural basis of multidrug transport by the acrb multidrug efflux pump in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1T9U
Type
protein
Length
1,013 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Acriflavine resistance protein B
UniProt
P31224
Ligands
CPF
Pockets
9 · best druggability 0.87

Structure

x-ray diffraction · 1 distinct chain · 46% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AAcriflavine resistance protein Bprotein101346% helix, 15% strandP31224

Ligands and binding sites

  • CPF · 1-cyclopropyl-6-fluoro-4-oxo-7-piperazin-1-yl-1,4-dihydroquinoline-3-carboxylic acid · ligand · 2 copies · chains A

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

Pockets

9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
110610.870.88130empty
21530.610.8525empty
32780.580.7834empty
42040.540.7827empty
51640.500.7825empty

Compared structures

  • 1T9U · Structural Basis of Multidrug Transport by the AcrB Multidrug Efflux Pump · the same entry in another collection · chain A against A, TM-score 1.00
  • P31224 · AlphaFold monomer V2.0 prediction for multidrug efflux pump subunit acrb (P31224) · a predicted model of the same protein · chain A against A, TM-score 0.95

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