› 5b5s

X-ray diffraction
1.5Å resolution

Crystal structure of a carbohydrate esterase family 3 from Talaromyces cellulolyticus

Released:
DOI: 10.2210/pdb5b5s/pdb
PDB entry 5b5s coloured by chain, front view.
PDB entry 5b5s coloured by chain, side view.
PDB entry 5b5s coloured by chain, top view.
Source organism: Talaromyces pinophilus
Primary publication:
Crystal structure of an acetylesterase from Talaromyces cellulolyticus and the importance of a disulfide bond near the active site.
Watanabe M, Fukada H, Inoue H, Ishikawa K
FEBS Lett 589 1200-6 (2015)
PMID: 25825334

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-100850 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
CBM1 domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 207 amino acids
Theoretical weight: 22.52 KDa
Source organism: Talaromyces pinophilus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0A8IBJ8 (Residues: 21-226; Coverage: 78%)
Gene names: TCE0_004r00149, axe
Sequence domains: GDSL-like Lipase/Acylhydrolase family
Structure domains: SGNH hydrolase

Ligands and Environments

4 bound ligands:
Ligand BOG 1 x BOG
Ligand CA 1 x CA
Ligand GOL 2 x GOL
Ligand SO3 1 x SO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P41212
Unit cell:
a: 70.905Å b: 70.905Å c: 87.093Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.148 0.145 0.203
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

The SGNH hydrolase family: a template for carbohydrate diversity.
Anderson et al. (2022)
3 other articles

5 mentions without citation

Acetylation of Surface Carbohydrates in Bacterial Pathogens Requires Coordinated Action of a Two-Domain Membrane-Bound Acyltransferase.
Pearson et al. (2020)
4 more