› 1eqp

X-ray diffraction
1.9Å resolution

EXO-B-(1,3)-GLUCANASE FROM CANDIDA ALBICANS

Released:
DOI: 10.2210/pdb1eqp/pdb
PDB entry 1eqp coloured by chain, front view.
PDB entry 1eqp coloured by chain, side view.
PDB entry 1eqp coloured by chain, top view.
Source organism: Candida albicans
Primary publication:
Minor structural consequences of alternative CUG codon usage (Ser for Leu) in Candida albicans exoglucanase.
Cutfield JF, Sullivan PA, Cutfield SM
Protein Eng 13 735-8 (2000)
PMID: 11112513

Function and Biology Details

Reaction catalysed: 
Successive hydrolysis of beta-D-glucose units from the non-reducing ends of (1->3)-beta-D-glucans, releasing alpha-glucose
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-151564 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glucan 1,3-beta-glucosidase Chain: A
Molecule details ›
Chain: A
Length: 394 amino acids
Theoretical weight: 45.24 KDa
Source organism: Candida albicans
UniProt:
  • Canonical: P29717 (Residues: 45-438; Coverage: 95%)
Gene names: CAALFM_C102990CA, Ca49C10.05, CaO19.10507, CaO19.2990, EXG, EXG1, XOG, XOG1
Sequence domains: Cellulase (glycosyl hydrolase family 5)
Structure domains: Glycosidases

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P212121
Unit cell:
a: 60.1Å b: 65.3Å c: 96.4Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.154 0.156 0.195

Quick links

Citations

1 review citation

Candida albicans cell wall proteins.
Chaffin WL. (2008)
10 other articles

3 mentions without citation

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