› 3u37

X-ray diffraction
2.1Å resolution

An Acetyl Xylan Esterase (Est2A) from the Rumen Bacterium Butyrivibrio proteoclasticus.

Released:
DOI: 10.2210/pdb3u37/pdb
PDB entry 3u37 coloured by chain, front view.
PDB entry 3u37 coloured by chain, side view.
PDB entry 3u37 coloured by chain, top view.
Source organism: Butyrivibrio proteoclasticus B316
Primary publication:
Structure and function of an acetyl xylan esterase (Est2A) from the rumen bacterium Butyrivibrio proteoclasticus.
Till M, Goldstone DC, Attwood GT, Moon CD, Kelly WJ, Arcus VL
Proteins 81 911-7 (2013)
PMID: 23345031

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo tetramer
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-122683 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Acetyl-xylan esterase Est2A Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 408 amino acids
Theoretical weight: 46.26 KDa
Source organism: Butyrivibrio proteoclasticus B316
Expression system: Escherichia coli
UniProt:
  • Canonical: E0RVY7 (Residues: 1-376; Coverage: 100%)
Gene names: bpr_I2939, est2A
Sequence domains: GDSL-like Lipase/Acylhydrolase
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand ACY 10 x ACY
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P1
Unit cell:
a: 96.128Å b: 90.282Å c: 99.175Å
α: 99.8° β: 90.21° γ: 92.56°
R-values:
R R work R free
0.208 0.206 0.242
Expression system: Escherichia coli

Quick links

Citations

8 citation in other articles

Active site architecture of an acetyl xylan esterase indicates a novel cold adaptation strategy.
Zhang et al. (2021)
7 more

7 mentions without citation

The SGNH hydrolase family: a template for carbohydrate diversity.
Anderson et al. (2022)
6 more