› 6hl7

X-ray diffraction
2.5Å resolution

Crystal structure of truncated aspartate transcarbamoylase from Plasmodium falciparum with mutated active site (R109A/K138A) and N-carbamoyl-L-phosphate bound

Released:
DOI: 10.2210/pdb6hl7/pdb
PDB entry 6hl7 coloured by chain, front view.
PDB entry 6hl7 coloured by chain, side view.
PDB entry 6hl7 coloured by chain, top view.
Source organism: Plasmodium falciparum
Primary publication:
Molecular Target Validation of Aspartate Transcarbamoylase from Plasmodium falciparum by Torin 2.
Bosch SS, Lunev S, Batista FA, Linzke M, Kronenberger T, Dömling ASS, Groves MR, Wrenger C
ACS Infect Dis 6 986-999 (2020)
PMID: 32129597

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-127545 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
aspartate carbamoyltransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 348 amino acids
Theoretical weight: 40.12 KDa
Source organism: Plasmodium falciparum
Expression system: Escherichia coli
UniProt:
  • Canonical: O15804 (Residues: 37-375; Coverage: 90%)
Gene name: ATCase
Sequence domains:
Structure domains: Aspartate/ornithine carbamoyltransferase

Ligands and Environments

1 bound ligand:
Ligand CP 2 x CP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: C2
Unit cell:
a: 148.001Å b: 89.715Å c: 121.642Å
α: 90° β: 122.17° γ: 90°
R-values:
R R work R free
0.207 0.204 0.258
Expression system: Escherichia coli

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Citations

1 review citation

Novel Highlight in Malarial Drug Discovery: Aspartate Transcarbamoylase.
Wang et al. (2022)
3 other articles