› 5w95

X-ray diffraction
1.72Å resolution

Mtb Rv3802c with PEG bound

Released:
DOI: 10.2210/pdb5w95/pdb
PDB entry 5w95 coloured by chain, front view.
PDB entry 5w95 coloured by chain, side view.
PDB entry 5w95 coloured by chain, top view.
Source organism: Mycobacterium tuberculosis
Primary publication:
Structural basis for lipid binding and mechanism of the Mycobacterium tuberculosis Rv3802 phospholipase.
Goins CM, Schreidah CM, Dajnowicz S, Ronning DR
J Biol Chem 293 1363-1372 (2018)
PMID: 29247008

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129454 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Carboxylesterase/lipase Culp6 Chains: A, B
Molecule details ›
Chains: A, B
Length: 285 amino acids
Theoretical weight: 30.3 KDa
Source organism: Mycobacterium tuberculosis
Expression system: Escherichia coli
UniProt:
  • Canonical: O53581 (Residues: 70-336; Coverage: 80%)
Gene names: Rv3802c, cut6
Sequence domains: Cutinase
Structure domains: alpha/beta hydrolase

Ligands and Environments

1 bound ligand:
Ligand 1PE 4 x 1PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P212121
Unit cell:
a: 57.188Å b: 91.3Å c: 101.391Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.158 0.183
Expression system: Escherichia coli

Quick links

Citations

3 citation in other articles

Identification of potential lipid biomarkers for active pulmonary tuberculosis using ultra-high-performance liquid chromatography-tandem mass spectrometry.
Han et al. (2021)
2 more

2 mentions without citation

Characterization of Tetrahydrolipstatin and Stereoderivatives on the Inhibition of Essential Mycobacterium tuberculosis Lipid Esterases.
Goins et al. (2018)
1 more