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X-ray diffraction
1.98Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-109797 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative esterase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 275 amino acids
Theoretical weight: 31.62 KDa
Source organism: Bacteroides intestinalis DSM 17393
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: B3CET1 (Residues: 21-294; Coverage: 100%)
Gene name: BACINT_04212
Sequence domains: Putative esterase

Ligands and Environments

2 bound ligands:
Ligand CA 8 x CA
Ligand IPA 18 x IPA
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 127.92Å b: 135.79Å c: 172.59Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.167 0.198
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

A mini review of xylanolytic enzymes with regards to their synergistic interactions during hetero-xylan degradation.
Malgas et al. (2019)
7 other articles

12 mentions without citation

Recent Advances and Future Prospects in Spark Plasma Sintered Alumina Hybrid Nanocomposites.
Saheb et al. (2019)
11 more