2es4

X-ray diffraction
1.85Å resolution

Crystal structure of the Burkholderia glumae lipase-specific foldase in complex with its cognate lipase

Released:

Function and Biology Details

Reaction catalysed:
Triacylglycerol + H(2)O = diacylglycerol + a carboxylate
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
hetero dimer (preferred)
hetero octamer
PDBe Complex ID:
PDB-CPX-145127 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Triacylglycerol lipase Chains: A, B
Molecule details ›
Chains: A, B
Length: 319 amino acids
Theoretical weight: 33.12 KDa
Source organism: Burkholderia glumae
UniProt:
  • Canonical: P0DUB8 (Residues: 40-358; Coverage: 100%)
Gene names: lip, lipA
Sequence domains: alpha/beta hydrolase fold
Structure domains: alpha/beta hydrolase
Lipase-specific foldase Chains: D, E
Molecule details ›
Chains: D, E
Length: 332 amino acids
Theoretical weight: 35.24 KDa
Source organism: Burkholderia glumae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q05490 (Residues: 42-352; Coverage: 88%)
Gene names: lifO, lipB
Sequence domains: Proteobacterial lipase chaperone protein

Ligands and Environments

2 bound ligands:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-2
Spacegroup: C2
Unit cell:
a: 183Å b: 75.7Å c: 116.6Å
α: 90° β: 117.6° γ: 90°
R-values:
R R work R free
0.199 0.199 0.219
Expression system: Escherichia coli