› 4n4b

X-ray diffraction
1.44Å resolution

Crystal Structure of the alpha-L-arabinofuranosidase PaAbf62A from Podospora anserina

Released:
DOI: 10.2210/pdb4n4b/pdb
PDB entry 4n4b coloured by chain, front view.
PDB entry 4n4b coloured by chain, side view.
PDB entry 4n4b coloured by chain, top view.
Source organism: Podospora anserina
Primary publication:
First structural insights into α-L-arabinofuranosidases from the two GH62 glycoside hydrolase subfamilies.
Siguier B, Haon M, Nahoum V, Marcellin M, Burlet-Schiltz O, Coutinho PM, Henrissat B, Mourey L, O'Donohue MJ, Berrin JG, Tranier S, Dumon C
J Biol Chem 289 5261-73 (2014)
PMID: 24394409

Function and Biology Details

Reaction catalysed: 
Hydrolysis of terminal non-reducing alpha-L-arabinofuranoside residues in alpha-L-arabinosides
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-122825 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-L-arabinofuranosidase Chain: A
Molecule details ›
Chain: A
Length: 360 amino acids
Theoretical weight: 40.2 KDa
Source organism: Podospora anserina
Expression system: Komagataella pastoris
UniProt:
  • Canonical: E2GHW5 (Residues: 1-337; Coverage: 100%)
Sequence domains: Glycosyl hydrolase family 62
Structure domains: Glycosyl hydrolase domain; family 43

Ligands and Environments

4 bound ligands:
Ligand CA 1 x CA
Ligand EPE 1 x EPE
Ligand TRS 1 x TRS
Ligand 1PE 1 x 1PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2
Unit cell:
a: 102.41Å b: 66.83Å c: 60.57Å
α: 90° β: 117.39° γ: 90°
R-values:
R R work R free
0.129 0.128 0.152
Expression system: Komagataella pastoris

Quick links

Citations

3 review citations

Insights into the mechanism of enzymatic hydrolysis of xylan.
Moreira et al. (2016)
2 more

1 mention without citation

First structural insights into α-L-arabinofuranosidases from the two GH62 glycoside hydrolase subfamilies.
Siguier et al. (2014)