4r76

X-ray diffraction
2.5Å resolution

Structure of the m17 leucyl aminopeptidase from malaria complexed with a hydroxamic acid-based inhibitor

Released:

Function and Biology Details

Reactions catalysed:
Release of N-terminal proline from a peptide.
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:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Leucine 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: 528 amino acids
Theoretical weight: 58.71 KDa
Source organism: Plasmodium falciparum FcB1/Columbia
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q8IL11 (Residues: 84-605; Coverage: 86%)
Gene names: LAP, PF3D7_1446200
Sequence domains: Cytosol aminopeptidase family, catalytic domain
Structure domains:

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX2
Spacegroup: P212121
Unit cell:
a: 174.041Å b: 177.408Å c: 231.77Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.207 0.248
Expression system: Escherichia coli BL21