› 5lnq

X-ray diffraction
1.98Å resolution

Crystal structure of SCP2 thiolase from Leishmania mexicana. Complex of the C123A mutant with acetoacetyl-CoA.

Released:
DOI: 10.2210/pdb5lnq/pdb
PDB 5lnq coloured by chain and viewed from the front.
PDB 5lnq coloured by chain and viewed from the side.
PDB 5lnq coloured by chain and viewed from the top.
Source organism: Leishmania mexicana
Primary publication:
Crystallographic substrate binding studies of Leishmania mexicana SCP2-thiolase (type-2): unique features of oxyanion hole-1.
Harijan RK, Kiema TR, Syed SM, Qadir I, Mazet M, Bringaud F, Michels PA, Wierenga RK
Protein Eng. Des. Sel. (2017)
PMID: 28062645

Function and Biology Details

Reaction catalysed: 
(1a) [acetyl-CoA C-acyltransferase]-S-acyl-L-cyteine + acetyl-CoA = 3-oxoacyl-CoA + [acetyl-CoA C-acyltransferase]-L-cyteine
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
3-ketoacyl-CoA thiolase-like protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 457 amino acids
Theoretical weight: 49.23 KDa
Source organism: Leishmania mexicana
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: E9AW84 (Residues: 1-441; Coverage: 100%)
Gene name: LMXM_23_0690
Sequence domains:
Structure domains: Peroxisomal Thiolase; Chain A, domain 1

Ligands and Environments


Cofactor: Ligand CAA 3 x CAA
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 74.141Å b: 89.804Å c: 123.716Å
α: 90° β: 104.76° γ: 90°
R-values:
R R work R free
0.191 0.189 0.226
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

The 3-ketoacyl-CoA thiolase: an engineered enzyme for carbon chain elongation of chemical compounds.
Liu et al. (2020)