› 3vzm

X-ray diffraction
1.86Å resolution

Crystal structure of the Bacillus circulans endo-beta-(1,4)-xylanase (BcX) E172H mutant with Glu78 covalently bonded to 2-deoxy-2-fluoro-xylobiose

Released:
DOI: 10.2210/pdb3vzm/pdb
PDB entry 3vzm coloured by chain, front view.
PDB entry 3vzm coloured by chain, side view.
PDB entry 3vzm coloured by chain, top view.
Source organism: Niallia circulans
Primary publication:
Strategies for modulating the pH-dependent activity of a family 11 glycoside hydrolase.
Ludwiczek ML, D'Angelo I, Yalloway GN, Brockerman JA, Okon M, Nielsen JE, Strynadka NC, Withers SG, McIntosh LP
Biochemistry 52 3138-56 (2013)
PMID: 23578322

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-140770 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Endo-1,4-beta-xylanase Chain: A
Molecule details ›
Chain: A
Length: 185 amino acids
Theoretical weight: 20.42 KDa
Source organism: Niallia circulans
Expression system: Escherichia coli
UniProt:
  • Canonical: P09850 (Residues: 29-213; Coverage: 100%)
Gene name: xlnA
Sequence domains: Glycosyl hydrolases family 11
Structure domains: Jelly Rolls

Ligands and Environments

Carbohydrate polymer : NEW Components: DFX, XYP
Carbohydrate polymer
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 43.451Å b: 52.387Å c: 77.768Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.172 0.254
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Classification, mode of action and production strategy of xylanase and its application for biofuel production from water hyacinth.
Uday et al. (2016)
1 more