› 6eee

X-ray diffraction
2.3Å resolution

X-ray crystal structure of Pf-M17 in complex with inhibitor (6k) and regulatory zinc ion

Released:
DOI: 10.2210/pdb6eee/pdb
PDB entry 6eee coloured by chain, front view.
PDB entry 6eee coloured by chain, side view.
PDB entry 6eee coloured by chain, top view.
Source organism: Plasmodium falciparum HB3
Primary publication:
Hydroxamic Acid Inhibitors Provide Cross-Species Inhibition of Plasmodium M1 and M17 Aminopeptidases.
Vinh NB, Drinkwater N, Malcolm TR, Kassiou M, Lucantoni L, Grin PM, Butler GS, Duffy S, Overall CM, Avery VM, Scammells PJ, McGowan S
J Med Chem 62 622-640 (2019)
PMID: 30537832

Function and Biology Details

Reaction catalysed: 
Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-102353 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
leucyl aminopeptidase Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 519 amino acids
Theoretical weight: 57.56 KDa
Source organism: Plasmodium falciparum HB3
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0L7KHE6 (Residues: 87-605; Coverage: 86%)
Gene name: PFHG_04072
Sequence domains: Cytosol aminopeptidase family, catalytic domain
Structure domains:

Ligands and Environments

8 bound ligands:
Ligand J4V 12 x J4V
Ligand CO3 12 x CO3
Ligand ZN 12 x ZN
Ligand SO4 31 x SO4
Ligand DMS 6 x DMS
Ligand 1PE 23 x 1PE
Ligand EDO 14 x EDO
Ligand 2PE 1 x 2PE
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P212121
Unit cell:
a: 173.68Å b: 177.395Å c: 229.445Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.193 0.246
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Structural Insights Into Key Plasmodium Proteases as Therapeutic Drug Targets.
Mishra et al. (2019)
1 more