› 3ro8

X-ray diffraction
1.34Å resolution

Crystal structure of the catalytic domain of XynA1 from Paenibacillus sp. JDR-2

Released:
DOI: 10.2210/pdb3ro8/pdb
PDB entry 3ro8 coloured by chain, front view.
PDB entry 3ro8 coloured by chain, side view.
PDB entry 3ro8 coloured by chain, top view.
Source organism: Paenibacillus sp. JDR-2
Primary publication:
Novel structural features of xylanase A1 from Paenibacillus sp. JDR-2.
St John FJ, Preston JF, Pozharski E
J Struct Biol 180 303-11 (2012)
PMID: 23000703

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-111558 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase A Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 341 amino acids
Theoretical weight: 38.4 KDa
Source organism: Paenibacillus sp. JDR-2
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: C6CRV0 (Residues: 518-851; Coverage: 23%)
Gene names: Pjdr2_0221, xynA, xynA1
Sequence domains: Glycosyl hydrolase family 10
Structure domains: Glycosidases

Ligands and Environments

2 bound ligands:
Ligand MG 11 x MG
Ligand CL 9 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL7-1
Spacegroup: P21
Unit cell:
a: 82.072Å b: 93.172Å c: 182.947Å
α: 90° β: 99.96° γ: 90°
R-values:
R R work R free
0.144 0.142 0.185
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 citation in other articles

Multidomain, Surface Layer-associated Glycoside Hydrolases Contribute to Plant Polysaccharide Degradation by Caldicellulosiruptor Species.
Conway et al. (2016)
7 more