› 3w25

X-ray diffraction
1.32Å resolution

The high-resolution crystal structure of TsXylA, intracellular xylanase from /Thermoanaerobacterium saccharolyticum JW/SL-YS485/: the complex of the E146A mutant with xylobiose

Released:
DOI: 10.2210/pdb3w25/pdb
PDB entry 3w25 coloured by chain, front view.
PDB entry 3w25 coloured by chain, side view.
PDB entry 3w25 coloured by chain, top view.
Source organism: Thermoanaerobacterium saccharolyticum JW/SL-YS485
Primary publication:
Structural and functional analyses of catalytic domain of GH10 xylanase from Thermoanaerobacterium saccharolyticum JW/SL-YS485.
Han X, Gao J, Shang N, Huang CH, Ko TP, Chen CC, Chan HC, Cheng YS, Zhu Z, Wiegel J, Luo W, Guo RT, Ma Y
Proteins 81 1256-65 (2013)
PMID: 23508990

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-125103 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Beta-xylanase Chain: A
Molecule details ›
Chain: A
Length: 336 amino acids
Theoretical weight: 38.01 KDa
Source organism: Thermoanaerobacterium saccharolyticum JW/SL-YS485
Expression system: Escherichia coli
UniProt:
  • Canonical: I3VVC1 (Residues: 349-684; Coverage: 24%)
Gene name: Tsac_1459
Sequence domains: Glycosyl hydrolase family 10
Structure domains: Glycosidases

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P21212
Unit cell:
a: 77.112Å b: 118.607Å c: 45.362Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.162 0.184
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Microbial application of thermophilic Thermoanaerobacterium species in lignocellulosic biorefinery.
Wu et al. (2021)
2 other articles

2 mentions without citation

Highly active enzymes by automated combinatorial backbone assembly and sequence design.
Lapidoth et al. (2018)
1 more