› 1qoz

X-ray diffraction
1.9Å resolution

Catalytic core domain of acetyl xylan esterase from Trichoderma reesei

Released:
DOI: 10.2210/pdb1qoz/pdb
PDB entry 1qoz coloured by chain, front view.
PDB entry 1qoz coloured by chain, side view.
PDB entry 1qoz coloured by chain, top view.
Source organism: Trichoderma reesei
Primary publication:
Three-dimensional structure of the catalytic core of acetylxylan esterase from Trichoderma reesei: insights into the deacetylation mechanism.
Hakulinen N, Tenkanen M, Rouvinen J
J Struct Biol 132 180-90 (2000)
PMID: 11243887

Function and Biology Details

Reaction catalysed: 
Deacetylation of xylans and xylo-oligosaccharides
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-189171 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylxylan esterase Chains: A, B
Molecule details ›
Chains: A, B
Length: 207 amino acids
Theoretical weight: 21.01 KDa
Source organism: Trichoderma reesei
UniProt:
  • Canonical: Q99034 (Residues: 32-238; Coverage: 73%)
Gene name: axe1
Sequence domains: Cutinase
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand NAG 2 x NAG
1 modified residue:
Ligand PCA 2 x PCA

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P1
Unit cell:
a: 50.3Å b: 61Å c: 40Å
α: 107.7° β: 113.5° γ: 98.8°
R-values:
R R work R free
0.186 0.186 0.247

Quick links

Citations

2 review citations

Microbial carbohydrate esterases deacetylating plant polysaccharides.
Biely P. (2012)
1 more

5 mentions without citation

New insights into the mycobacterial PE and PPE proteins provide a framework for future research.
Ates LS. (2020)
4 more