› 3ug3

X-ray diffraction
1.8Å resolution

Crystal structure of alpha-L-arabinofuranosidase from Thermotoga maritima ligand free form

Released:
DOI: 10.2210/pdb3ug3/pdb
PDB entry 3ug3 coloured by chain, front view.
PDB entry 3ug3 coloured by chain, side view.
PDB entry 3ug3 coloured by chain, top view.
Source organism: Thermotoga maritima
Primary publication:
Crystal structures of glycoside hydrolase family 51 α-L-arabinofuranosidase from Thermotoga maritima.
Im DH, Kimura K, Hayasaka F, Tanaka T, Noguchi M, Kobayashi A, Shoda S, Miyazaki K, Wakagi T, Fushinobu S
Biosci Biotechnol Biochem 76 423-8 (2012)
PMID: 22313787

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:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-194494 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Alpha-L-arabinofuranosidase C-terminal domain-containing protein Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 504 amino acids
Theoretical weight: 57.41 KDa
Source organism: Thermotoga maritima
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9WYB7 (Residues: 1-484; Coverage: 100%)
Gene name: TM_0281
Sequence domains: Alpha-L-arabinofuranosidase C-terminal domain
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand TRS 6 x TRS
Ligand EDO 51 x EDO
Ligand NA 1 x NA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: P21
Unit cell:
a: 101.515Å b: 160.647Å c: 155.735Å
α: 90° β: 91.75° γ: 90°
R-values:
R R work R free
0.176 0.175 0.197
Expression system: Escherichia coli

Quick links

Citations

2 review citations

β-xylosidases and α-L-arabinofuranosidases: accessory enzymes for arabinoxylan degradation.
Lagaert et al. (2014)
1 more

3 mentions without citation

A novel bifunctional GH51 exo-α-l-arabinofuranosidase/endo-xylanase from Alicyclobacillus sp. A4 with significant biomass-degrading capacity.
Yang et al. (2015)
2 more