› 5ilq

X-ray diffraction
2.5Å resolution

Crystal structure of truncated unliganded Aspartate Transcarbamoylase from Plasmodium falciparum

Released:
DOI: 10.2210/pdb5ilq/pdb
PDB entry 5ilq coloured by chain, front view.
PDB entry 5ilq coloured by chain, side view.
PDB entry 5ilq coloured by chain, top view.
Source organism: Plasmodium falciparum 3D7
Primary publication:
Crystal structure of truncated aspartate transcarbamoylase from Plasmodium falciparum.
Lunev S, Bosch SS, Batista Fde A, Wrenger C, Groves MR
Acta Crystallogr F Struct Biol Commun 72 523-33 (2016)
PMID: 27380369

Function and Biology Details

Reaction catalysed: 
Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-105431 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
aspartate carbamoyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 349 amino acids
Theoretical weight: 40.35 KDa
Source organism: Plasmodium falciparum 3D7
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A5K1K910 (Residues: 37-375; Coverage: 90%)
Gene name: PF3D7_1344800
Sequence domains:
Structure domains: Aspartate/ornithine carbamoyltransferase

Ligands and Environments

2 bound ligands:
Ligand GOL 3 x GOL
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P21
Unit cell:
a: 86.98Å b: 103.8Å c: 87.11Å
α: 90° β: 117.68° γ: 90°
R-values:
R R work R free
0.208 0.208 0.25
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

1 review citation

Amino Acid Metabolism in Apicomplexan Parasites.
Krishnan et al. (2021)
1 other article

3 mentions without citation

Novel Highlight in Malarial Drug Discovery: Aspartate Transcarbamoylase.
Wang et al. (2022)
2 more