3h3i

X-ray diffraction
2.2Å resolution

CRYSTAL STRUCTURE OF A PUTATIVE LIPID BINDING PROTEIN (BT_2261) FROM BACTEROIDES THETAIOTAOMICRON VPI-5482 AT 2.20 A RESOLUTION

Released:
Entry author: Joint Center for Structural Genomics (JCSG)

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-183691 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lipid-binding hydrolase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 150 amino acids
Theoretical weight: 16.79 KDa
Source organism: Bacteroides thetaiotaomicron VPI-5482
Expression system: Escherichia coli
UniProt:
  • Canonical: Q8A5H8 (Residues: 18-166; Coverage: 100%)
Gene name: BT_2261
Sequence domains: Lipid-binding putative hydrolase
Structure domains: Lipocalin

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL11-1
Spacegroup: P3212
Unit cell:
a: 67.383Å b: 67.383Å c: 186.164Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.189 0.187 0.232
Expression system: Escherichia coli