› 5ay7

X-ray diffraction
2.15Å resolution

A psychrophilic glycoside hydrolase family 10 endo-beta-1,4-xylanase

Released:
DOI: 10.2210/pdb5ay7/pdb
PDB entry 5ay7 coloured by chain, front view.
PDB entry 5ay7 coloured by chain, side view.
PDB entry 5ay7 coloured by chain, top view.
Source organism: Aegilops speltoides subsp. speltoides
Primary publication:
Structural insight into potential cold adaptation mechanism through a psychrophilic glycoside hydrolase family 10 endo-β-1,4-xylanase.
Zheng Y, Li Y, Liu W, Chen CC, Ko TP, He M, Xu Z, Liu M, Luo H, Guo RT, Yao B, Ma Y
J Struct Biol 193 206-211 (2016)
PMID: 26719223

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-102993 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GH10 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 355 amino acids
Theoretical weight: 41.22 KDa
Source organism: Aegilops speltoides subsp. speltoides
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: A0A140UHL2 (Residues: 1-341; Coverage: 100%)
Sequence domains: Glycosyl hydrolase family 10
Structure domains: Glycosidases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P21
Unit cell:
a: 59.434Å b: 78.346Å c: 89.296Å
α: 90° β: 103.15° γ: 90°
R-values:
R R work R free
0.195 0.192 0.257
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

Quick links

Citations

3 review citations

Extremophilic Prokaryotic Endoxylanases: Diversity, Applicability, and Molecular Insights.
Verma D. (2021)
2 more

3 mentions without citation

Discovery, Molecular Mechanisms, and Industrial Applications of Cold-Active Enzymes.
Santiago et al. (2016)
2 more