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Crystal structure of endo-1,4-beta-xylanase from caldicellulosiruptor owensensis

Analyse Crystal structure of endo-1,4-beta-xylanase from caldicellulosiruptor owensensis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
5Y3X
Type
protein
Length
1,974 residues
Chains
6
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Beta-xylanase
EC
3.2.1.8
UniProt
E4Q2A4
Pockets
14 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 40% helix, 20% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
A, B, C, D, E, FBeta-xylanase (EC 3.2.1.8)protein32940% helix, 20% strandE4Q2A4

Pockets

14 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.

PocketVolume (ų)DruggabilityBuriednessLining residuesInside
111320.790.81111empty
27920.770.8184empty
39680.760.79101empty
46450.740.8057empty
52310.550.7834empty

Interfaces

8 interfaces between chains.

  • D–F · 626 Ų buried · 7 hydrogen bonds · protein-protein
  • A–B · 610 Ų buried · 7 hydrogen bonds · protein-protein
  • D–E · 593 Ų buried · 8 hydrogen bonds · protein-protein
  • A–E · 581 Ų buried · 8 hydrogen bonds · protein-protein
  • B–D · 559 Ų buried · 11 hydrogen bonds · protein-protein

Compared structures

  • 5Y3X · Crystal structure of endo-1,4-beta-xylanase from Caldicellulosiruptor owensensis · the same entry in another collection · chain A against A, TM-score 1.00

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