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Crystal structure of reducing-end-xylose releasing exo-oligoxylanase Y198F mutant

Analyse Crystal structure of reducing-end-xylose releasing exo-oligoxylanase Y198F… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3A3V
Type
protein
Length
376 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v2 / PDB Bank
Contract
0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner
0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution
1.39
Source
Bacillus halodurans
Molecule
Xylanase Y
EC
3.2.1.156
UniProt
Q9KB30
Ligands
NI
Pockets
2 · best druggability 0.56

Structure

x-ray diffraction · resolution 1.39 · 1 distinct chain · 50% helix, 8% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AXylanase Y (EC 3.2.1.156)protein37650% helix, 8% strandQ9KB30

Ligands and binding sites

  • NI · Nickel (II) ion · metal · chains A
  • GOL · Glycerol · additive · 4 copies · 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
12560.560.7834GOL
2570.430.8318empty

Compared structures

  • 3A3V · Crystal structure of reducing-end-xylose releasing exo-oligoxylanase Y198F mutant · the same entry in another collection · chain A against A, TM-score 1.00
  • Q9KB30 · AlphaFold monomer V2.0 prediction for reducing end xylose-releasing exo-oligoxylanase… · a predicted model of the same protein · chain A against A, TM-score 1.00

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