› 2axe

X-ray diffraction
1.8Å resolution

IODINATED COMPLEX OF ACETYL XYLAN ESTERASE AT 1.80 ANGSTROMS

Released:
DOI: 10.2210/pdb2axe/pdb
PDB entry 2axe coloured by chain, front view.
PDB entry 2axe coloured by chain, side view.
PDB entry 2axe coloured by chain, top view.
Source organism: Talaromyces purpureogenus
Primary publication:
Determination of a protein structure by iodination: the structure of iodinated acetylxylan esterase.
Ghosh D, Erman M, Sawicki M, Lala P, Weeks DR, Li N, Pangborn W, Thiel DJ, Jörnvall H, Gutierrez R, Eyzaguirre J
Acta Crystallogr D Biol Crystallogr 55 779-84 (1999)
PMID: 10089308

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: 21.17 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

1 bound ligand:
Ligand SO4 1 x SO4
1 modified residue:
Ligand TYI 2 x TYI

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH2R
Spacegroup: P212121
Unit cell:
a: 34.9Å b: 61.278Å c: 72.538Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 not available 0.237

Quick links

Citations

3 review citations

Alpha/beta hydrolase fold enzymes: the family keeps growing.
Nardini et al. (1999)
2 more

1 mention without citation

Towards the prediction of protein interaction partners using physical docking.
Wass et al. (2011)