› 1us3

X-ray diffraction
1.85Å resolution

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 domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176818 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-beta-1,4-xylanase Xyn10C Chain: A
Molecule details ›
Chain: A
Length: 530 amino acids
Theoretical weight: 58.21 KDa
Source organism: Cellvibrio japonicus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q59675 (Residues: 86-606; Coverage: 89%)
Gene names: xyn10C, xynF
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand GOL 1 x GOL
Ligand TRS 1 x TRS
Ligand NA 2 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-4
Spacegroup: P212121
Unit cell:
a: 44.175Å b: 78.789Å c: 172.244Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.16 0.195
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Xylanases, xylanase families and extremophilic xylanases.
Collins et al. (2005)
5 more

6 mentions without citation

Distinct roles for carbohydrate-binding modules of glycoside hydrolase 10 (GH10) and GH11 xylanases from Caldicellulosiruptor sp. strain F32 in thermostability and catalytic efficiency.
Meng et al. (2015)
5 more