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Xylanase from penicillium simplicissimum, complex with xylose

Analyse Xylanase from penicillium simplicissimum, complex with xylose in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB
1B3V
Type
protein
Length
302 residues
Chains
1
Method
x-ray diffraction
Collection
MolNFT v1 / PDB
Contract
0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner
0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule
Protein (xylanase)
EC
3.2.1.8
UniProt
P56588
Ligands
XYP, XYS

Structure

x-ray diffraction · 1 distinct chain · 43% helix, 19% strand (DSSP).

ChainMoleculeTypeResiduesSecondary structureUniProt
AProtein (xylanase) (EC 3.2.1.8)protein30243% helix, 19% strandP56588

Ligands and binding sites

  • XYP · beta-D-xylopyranose · sugar · 3 copies · chains A
  • XYS · alpha-D-xylopyranose · sugar · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Modifications

Observed in the structure: 1 disulfide, 1 modified (disulfide, cyclization).

Compared structures

  • 1B3V · Xylanase from penicillium simplicissimum, complex with xylose · the same entry in another collection · chain A against A, TM-score 1.00
  • P56588 · AlphaFold monomer V2.0 prediction for endo-1,4-beta-xylanase (P56588) · a predicted model of the same protein · chain A against A, TM-score 1.00

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