3e0x

X-ray diffraction
1.45Å resolution

The crystal structure of a Lipase-esterase related protein from Clostridium acetobutylicum ATCC 824

Released:
Source organism: Clostridium acetobutylicum
Entry authors: Tan K, Sather A, Cobb G, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-188929 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
AB hydrolase-1 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 245 amino acids
Theoretical weight: 27.63 KDa
Source organism: Clostridium acetobutylicum
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q97KV0 (Residues: 1-242; Coverage: 100%)
Gene name: CA_C0816
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P21
Unit cell:
a: 44.611Å b: 75.153Å c: 68.206Å
α: 90° β: 97.89° γ: 90°
R-values:
R R work R free
0.145 0.143 0.185
Expression system: Escherichia coli BL21