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Xylanase C from aspergillus kawachii F131W mutant

Analyse Xylanase C from aspergillus kawachii F131W mutant in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
3RI9
Type
protein
Length
182 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Endo-1,4-beta-xylanase 3
EC
3.2.1.8
UniProt
P33557
Pockets
1 · best druggability 0.51

Structure

x-ray diffraction · 1 distinct chain · 10% helix, 63% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AEndo-1,4-beta-xylanase 3 (EC 3.2.1.8)protein18210% helix, 63% strandP33557

Pockets

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

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11960.510.7725empty

Modifications

Observed in the structure: 1 disulfide (disulfide).

Compared structures

  • 3RI9 · Xylanase C from Aspergillus kawachii F131W mutant · the same entry in another collection · chain A against A, TM-score 1.00
  • P33557 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase 3 (P33557) · a predicted model of the same protein · chain A against A, TM-score 0.99

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