› 1xyz

X-ray diffraction
1.4Å resolution

A COMMON PROTEIN FOLD AND SIMILAR ACTIVE SITE IN TWO DISTINCT FAMILIES OF BETA-GLYCANASES

Released:
DOI: 10.2210/pdb1xyz/pdb
PDB entry 1xyz coloured by chain, front view.
PDB entry 1xyz coloured by chain, side view.
PDB entry 1xyz coloured by chain, top view.
Source organism: Acetivibrio thermocellus
Primary publication:
A common protein fold and similar active site in two distinct families of beta-glycanases.
Dominguez R, Souchon H, Spinelli S, Dauter Z, Wilson KS, Chauvaux S, Béguin P, Alzari PM
Nat Struct Biol 2 569-76 (1995)
PMID: 7664125

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 domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-145316 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase Z Chains: A, B
Molecule details ›
Chains: A, B
Length: 347 amino acids
Theoretical weight: 39.43 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli
UniProt:
  • Canonical: P10478 (Residues: 491-837; Coverage: 43%)
Gene names: Cthe_1963, xynZ
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: EMBL/DESY, HAMBURG BEAMLINE X31
Spacegroup: P1
Unit cell:
a: 47.1Å b: 51.1Å c: 70.74Å
α: 100.54° β: 83.79° γ: 101.64°
R-values:
R R work R free
0.183 0.183 0.221
Expression system: Escherichia coli

Quick links

Citations

6 review citations

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

13 mentions without citation

Structure of mammalian AMPK and its regulation by ADP.
Xiao et al. (2011)
12 more