› 1wb5

X-ray diffraction
1.4Å resolution

S954A mutant of the feruloyl esterase module from clostridium thermocellum complexed with syringate

Released:
DOI: 10.2210/pdb1wb5/pdb
PDB entry 1wb5 coloured by chain, front view.
PDB entry 1wb5 coloured by chain, side view.
PDB entry 1wb5 coloured by chain, top view.
Source organism: Acetivibrio thermocellus
Primary publication:
Molecular determinants of substrate specificity in the feruloyl esterase module of xylanase 10B from Clostridium thermocellum.
Tarbouriech N, Prates JA, Fontes CM, Davies GJ
Acta Crystallogr D Biol Crystallogr 61 194-7 (2005)
PMID: 15681871

Function and Biology Details

Reaction catalysed: 
Endohydrolysis of (1->4)-beta-D-xylosidic linkages in xylans
Biochemical function:
  • not assigned
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-156366 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Endo-1,4-beta-xylanase Y Chains: A, B
Molecule details ›
Chains: A, B
Length: 297 amino acids
Theoretical weight: 33.75 KDa
Source organism: Acetivibrio thermocellus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P51584 (Residues: 792-1077; Coverage: 27%)
Gene name: xynY
Sequence domains: Putative esterase
Structure domains: alpha/beta hydrolase

Ligands and Environments

4 bound ligands:
Ligand SYR 2 x SYR
Ligand GOL 4 x GOL
Ligand ACT 2 x ACT
Ligand CD 17 x CD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: P212121
Unit cell:
a: 64.933Å b: 108.631Å c: 112.969Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.119 0.118 0.139
Expression system: Escherichia coli BL21(DE3)

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Citations

1 review citation

Feruloyl esterases as biotechnological tools: current and future perspectives.
Fazary et al. (2007)
8 other articles