› 1g66

X-ray diffraction
0.9Å resolution

ACETYLXYLAN ESTERASE AT 0.90 ANGSTROM RESOLUTION

Released:
DOI: 10.2210/pdb1g66/pdb
PDB entry 1g66 coloured by chain, front view.
PDB entry 1g66 coloured by chain, side view.
PDB entry 1g66 coloured by chain, top view.
Source organism: Talaromyces purpureogenus
Primary publication:
Multiple conformations of catalytic serine and histidine in acetylxylan esterase at 0.90 A.
Ghosh D, Sawicki M, Lala P, Erman M, Pangborn W, Eyzaguirre J, Gutierrez R, Jornvall H, Thiel DJ
J Biol Chem 276 11159-66 (2001)
PMID: 11134051

Function and Biology Details

Reaction catalysed: 
Deacetylation of xylans and xylo-oligosaccharides
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129888 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetylxylan esterase 2 Chain: A
Molecule details ›
Chain: A
Length: 207 amino acids
Theoretical weight: 20.66 KDa
Source organism: Talaromyces purpureogenus
UniProt:
  • Canonical: O59893 (Residues: 28-234; Coverage: 95%)
Gene names: axe-2, axeII
Sequence domains: Cutinase
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
Ligand SO4 4 x SO4
Ligand GOL 4 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: CHESS BEAMLINE A1
Spacegroup: P212121
Unit cell:
a: 34.541Å b: 59.898Å c: 71.392Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.107 0.107 0.132

Quick links

Citations

3 review citations

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

9 mentions without citation

Hydration water and bulk water in proteins have distinct properties in radial distributions calculated from 105 atomic resolution crystal structures.
Chen et al. (2008)
8 more