› 7d89

X-ray diffraction
2.89Å resolution

Crystal structure of an inactivated double mutant (E182AE280A) of a novel thermostable GH10 xylanase XynA

Released:
DOI: 10.2210/pdb7d89/pdb
PDB entry 7d89 coloured by chain, front view.
PDB entry 7d89 coloured by chain, side view.
PDB entry 7d89 coloured by chain, top view.
Source organism: Bacillus sp. (in: Bacteria)
Primary publication:
Insights into the Catalytic Mechanism of a Novel XynA and Structure-Based Engineering for Improving Bifunctional Activities.
Xie W, Yu Q, Zhang R, Liu Y, Cao R, Wang S, Zhan R, Liu Z, Wang K, Wang C
Biochemistry 60 2071-2083 (2021)
PMID: 34156819

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-105166 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Beta-xylanase Chain: A
Molecule details ›
Chain: A
Length: 428 amino acids
Theoretical weight: 49.81 KDa
Source organism: Bacillus sp. (in: Bacteria)
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A4P8ESF9 (Residues: 1-408; Coverage: 100%)
Gene name: xyn10A
Sequence domains: Glycosyl hydrolase family 10

Ligands and Environments

1 bound ligand:
Ligand CA 2 x CA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P4122
Unit cell:
a: 110.193Å b: 110.193Å c: 84.983Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.235 0.232 0.279
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 citation in other articles

Biochemical and Thermodynamic Studies on a Novel Thermotolerant GH10 Xylanase from Bacillus safensis.
Glekas et al. (2022)
2 more