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› 3ebg

X-ray diffraction
2.1Å resolution

Structure of the M1 Alanylaminopeptidase from malaria

Released:
DOI: 10.2210/pdb3ebg/pdb
Model geometry
Fit model/data
PDB entry 3ebg coloured by chain, front view.
PDB entry 3ebg coloured by chain, side view.
PDB entry 3ebg coloured by chain, top view.
Source organism: Plasmodium falciparum FcB1/Columbia
Primary publication:
Structural basis for the inhibition of the essential Plasmodium falciparum M1 neutral aminopeptidase.
McGowan S, Porter CJ, Lowther J, Stack CM, Golding SJ, Skinner-Adams TS, Trenholme KR, Teuscher F, Donnelly SM, Grembecka J, Mucha A, Kafarski P, Degori R, Buckle AM, Gardiner DL, Whisstock JC, Dalton JP
Proc Natl Acad Sci U S A 106 2537-42 (2009)
PMID: 19196988

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:

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand MG 2 x MG
Ligand GOL 5 x GOL
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ELLIOTT GX-13
Spacegroup: P212121
Unit cell:
a: 75.656Å b: 108.684Å c: 118.399Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.173 0.17 0.22
Expression system: Escherichia coli

Quick links

Citations

16 review citations

Plasmodium falciparum neutral aminopeptidases: new targets for anti-malarials.
Skinner-Adams et al. (2010)
15 more

14 mentions without citation

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