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Structure of a periplasmic oligogalacturonide binding protein from Yersinia enterocolitica in complex with 4,5-unsaturated digalacturonic acid

Analyse Structure of a periplasmic oligogalacturonide binding protein from Yersinia… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
2UVI
Type
protein
Length
404 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
2.3
Source
YERSINIA ENTEROCOLITICA
Molecule
ABC type periplasmic sugar-binding protein
Ligands
ADA, AQA
Pockets
2 · best druggability 0.72

Structure

x-ray diffraction · resolution 2.3 · 1 distinct chain · 48% helix, 15% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AABC type periplasmic sugar-binding proteinprotein40448% helix, 15% strand—

Ligands and binding sites

  • ADA · alpha-D-galactopyranuronic acid · sugar · chains A
  • AQA · 4-deoxy-beta-L-threo-hex-4-enopyranuronic acid · sugar · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
14390.720.8252ADA, AQA
21010.360.7415empty

Compared structures

  • 2UVI · Structure of a periplasmic oligogalacturonide binding protein from yersinia… · the same entry in another collection · chain A against A, TM-score 1.00

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