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Crystal structure of GH10 family xylanase XYNAF1 from aspergillus fumigatus Z5

Analyse Crystal structure of GH10 family xylanase XYNAF1 from aspergillus fumigatus Z5 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
6JDT
Type
protein
Length
638 residues
Chains
2
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-xylanase
EC
3.2.1.8
UniProt
A0A0J5Q413
Ligands
NAG
Pockets
2 · best druggability 0.47

Structure

x-ray diffraction · 1 distinct chain · 44% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, BBeta-xylanase (EC 3.2.1.8)protein31944% helix, 20% strandA0A0J5Q413

Ligands and binding sites

  • NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 2 copies · chains A, B
  • MES · 2-(N-morpholino)-ethanesulfonic acid · additive · 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, 0 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
11360.470.7827empty
21220.440.7725empty

Interfaces

1 interface between chains.

  • A–B · 439 Ų buried · 5 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 disulfide, 2 glycan (disulfide, N-glycosylation).

Compared structures

  • 6JDT · Crystal structure of GH10 family xylanase XynAF1 from Aspergillus fumigatus Z5 · the same entry in another collection · chain A against A, TM-score 1.00

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