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Crystal structure of bacillus sp. GL1 xanthan lyase that acts on side chains of xanthan

Analyse Crystal structure of bacillus sp. GL1 xanthan lyase that acts on side chains of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1J0N
Type
protein
Length
752 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Xanthan lyase
EC
4.2.2.12
UniProt
Q9AQS0
Ligands
CEG, CA
Pockets
3 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 31% helix, 28% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AXanthan lyase (EC 4.2.2.12)protein75231% helix, 28% strandQ9AQS0

Ligands and binding sites

  • CEG · 4,6-O-[(1S)-1-carboxyethylidene]-beta-D-glucopyranose · ligand · chains A
  • CA · Calcium ion · metal · chains A

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

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111230.770.7979CEG
21610.430.7432empty
31030.370.7518empty

Compared structures

  • 1J0N · Crystal Structure of Bacillus sp. GL1 Xanthan Lyase that Acts on Side Chains of Xanthan · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9AQS0 · AlphaFold monomer V2.0 prediction for xanthan lyase (Q9AQS0) · a predicted model of the same protein · chain A against A, TM-score 1.00

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