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Crystal structures and biochemical characterization of the bacterial solute receptor acbh reveal an unprecedented exclusive substrate preference for B-D-galactopyranose

Analyse Crystal structures and biochemical characterization of the bacterial solute… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3OO9
Type
protein
Length
790 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
ABC transporter binding protein acbh
UniProt
Q27GR2
Ligands
SO4
Pockets
6 · best druggability 0.74

Structure

x-ray diffraction · 1 distinct chain · 52% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BABC transporter binding protein acbhprotein39552% helix, 15% strandQ27GR2

Ligands and binding sites

  • SO4 · Sulfate ion · ion · 17 copies · chains A, B
  • GOL · Glycerol · additive · 8 copies · chains A, B

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

Pockets

6 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
17280.740.8067SO4, GOL
23610.580.7542SO4, GOL
33180.560.7541GOL
41140.480.8019empty
51550.470.7724empty

Interfaces

1 interface between chains.

  • A–B · 557 Ų buried · 6 hydrogen bonds · protein-protein

Compared structures

  • 3OO9 · Crystal structures and biochemical characterization of the bacterial solute receptor AcbH… · the same entry in another collection · chain A against A, TM-score 1.00

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