X-ray diffraction
2.5Å resolution

Crystal structure of lipase/esterase (lp_2923) from Lactobacillus plantarum. Northeast Structural Genomics Consortium target LpR108

Entry authors: Forouhar F, Su M, Seetharaman J, Mao L, Janjua H, Xiao R, Ciccosanti C, Maglaqui M, Foote EL, Zhao L, Everett JK, Acton TB, Montelione GT, Tong L, Hunt JF, Northeast Structural Genomics Consortium (NESG)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Abhydrolase_3 domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 284 amino acids
Theoretical weight: 31.8 KDa
Source organism: Lactobacillus plantarum WCFS1
Expression system: Escherichia coli
  • Canonical: F9US10 (Residues: 1-276; Coverage: 100%)
Gene name: lp_2923
Structure domains: alpha/beta hydrolase

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X4C
Spacegroup: P212121
Unit cell:
a: 66.074Å b: 93.022Å c: 95.765Å
α: 90° β: 90° γ: 90°
R R work R free
0.217 0.216 0.263
Expression system: Escherichia coli