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Thermostabilization of the bacillus circulans xylanase, by the introduction of disulfide bonds

Analyse Thermostabilization of the bacillus circulans xylanase, by the introduction of… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1XNC
Type
protein
Length
185 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Xylanase
EC
3.2.1.8
UniProt
P09850
Pockets
1 · best druggability 0.48

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 62% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AXylanase (EC 3.2.1.8)protein1855% helix, 62% strandP09850

Pockets

1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11420.480.7825empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 1XNC · Thermostabilization of the bacillus circulans xylanase, by the introduction of disulfide… · the same entry in another collection · chain A against A, TM-score 1.00
  • P09850 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase (P09850) · a predicted model of the same protein · chain A against A, TM-score 0.99

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