› 4r5t

X-ray diffraction
1.98Å resolution

Structure of the m1 alanylaminopeptidase from malaria complexed with a hydroxamic acid-based inhibitor

Released:
DOI: 10.2210/pdb4r5t/pdb
PDB entry 4r5t coloured by chain, front view.
PDB entry 4r5t coloured by chain, side view.
PDB entry 4r5t coloured by chain, top view.
Source organism: Plasmodium falciparum FcB1/Columbia
Primary publication:
Two-pronged attack: dual inhibition of Plasmodium falciparum M1 and M17 metalloaminopeptidases by a novel series of hydroxamic acid-based inhibitors.
Mistry SN, Drinkwater N, Ruggeri C, Sivaraman KK, Loganathan S, Fletcher S, Drag M, Paiardini A, Avery VM, Scammells PJ, McGowan S
J Med Chem 57 9168-83 (2014)
PMID: 25299353

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: 896 amino acids
Theoretical weight: 104.6 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 DMS 2 x DMS
Ligand GOL 8 x GOL
Ligand R5T 1 x R5T
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: AUSTRALIAN SYNCHROTRON BEAMLINE MX1
Spacegroup: P212121
Unit cell:
a: 75.193Å b: 109.587Å c: 118.49Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.185 0.183 0.228
Expression system: Escherichia coli BL21

Quick links

Citations

4 review citations

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

1 mention without citation

Marine Invertebrates: A Promissory Still Unexplored Source of Inhibitors of Biomedically Relevant Metallo Aminopeptidases Belonging to the M1 and M17 Families.
Pascual Alonso et al. (2023)