› 5glp

X-ray diffraction
1.8Å resolution

Crystal structure of CoXyl43, GH43 beta-xylosidase/alpha-arabinofuranosidase from a compostmicrobial metagenome in complex with l-arabinose, calcium-bound form

Released:
DOI: 10.2210/pdb5glp/pdb
PDB entry 5glp coloured by chain, front view.
PDB entry 5glp coloured by chain, side view.
PDB entry 5glp coloured by chain, top view.
Source organism: uncultured bacterium
Primary publication:
Crystal structure of metagenomic β-xylosidase/ α-l-arabinofuranosidase activated by calcium.
Matsuzawa T, Kaneko S, Kishine N, Fujimoto Z, Yaoi K
J Biochem 162 173-181 (2017)
PMID: 28204531

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102201 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycoside hydrolase family 43 Chains: A, B
Molecule details ›
Chains: A, B
Length: 344 amino acids
Theoretical weight: 38.53 KDa
Source organism: uncultured bacterium
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0H5BL38 (Residues: 47-369; Coverage: 88%)
Gene name: coxyl43
Sequence domains: Glycosyl hydrolases family 43
Structure domains: Glycosyl hydrolase domain; family 43

Ligands and Environments

4 bound ligands:
Ligand CA 2 x CA
Ligand NA 2 x NA
Ligand ARA 4 x ARA
Ligand ACT 1 x ACT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P21
Unit cell:
a: 74.801Å b: 61.329Å c: 79.07Å
α: 90° β: 95.51° γ: 90°
R-values:
R R work R free
0.152 0.151 0.174
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

β-Xylosidases: Structural Diversity, Catalytic Mechanism, and Inhibition by Monosaccharides.
Rohman et al. (2019)
8 other articles