› 4k5p

X-ray diffraction
1.85Å resolution

Phosphonic Arginine Mimetics as Inhibitors of the M1 Aminopeptidases from Plasmodium falciparum

Released:
DOI: 10.2210/pdb4k5p/pdb
PDB entry 4k5p coloured by chain, front view.
PDB entry 4k5p coloured by chain, side view.
PDB entry 4k5p coloured by chain, top view.
Source organism: Plasmodium falciparum FcB1/Columbia
Primary publication:
Synthesis and structure-activity relationships of phosphonic arginine mimetics as inhibitors of the M1 and M17 aminopeptidases from Plasmodium falciparum.
Kannan Sivaraman K, Paiardini A, Sieńczyk M, Ruggeri C, Oellig CA, Dalton JP, Scammells PJ, Drag M, McGowan S
J Med Chem 56 5213-7 (2013)
PMID: 23713488

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-132164 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
p68 form Chain: A
Molecule details ›
Chain: A
Length: 895 amino acids
Theoretical weight: 104.46 KDa
Source organism: Plasmodium falciparum FcB1/Columbia
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: O96935 (Residues: 196-1084; Coverage: 84%)
Gene names: M1AAP, MAL13P1.56, PF3D7_1311800
Sequence domains:
Structure domains:

Ligands and Environments

4 bound ligands:
Ligand ZN 1 x ZN
Ligand GOL 2 x GOL
Ligand MG 2 x MG
Ligand 1OS 1 x 1OS
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 75.794Å b: 109.048Å c: 118.84Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.175 0.172 0.225
Expression system: Escherichia coli BL21

Quick links

Citations

6 review citations

M1 aminopeptidases as drug targets: broad applications or therapeutic niche?
Drinkwater et al. (2017)
5 more

2 mentions without citation

The Potential of Secondary Metabolites from Plants as Drugs or Leads against Protozoan Neglected Diseases-Part III: In-Silico Molecular Docking Investigations.
Ogungbe et al. (2016)
1 more