› 2pgf

X-ray diffraction
1.89Å resolution

Crystal structure of adenosine deaminase from Plasmodium vivax in complex with adenosine

Released:
DOI: 10.2210/pdb2pgf/pdb
PDB entry 2pgf coloured by chain, front view.
PDB entry 2pgf coloured by chain, side view.
PDB entry 2pgf coloured by chain, top view.
Source organism: Plasmodium vivax
Primary publication:
Structures of substrate- and inhibitor-bound adenosine deaminase from a human malaria parasite show a dramatic conformational change and shed light on drug selectivity.
Larson ET, Deng W, Krumm BE, Napuli A, Mueller N, Van Voorhis WC, Buckner FS, Fan E, Lauricella A, DeTitta G, Luft J, Zucker F, Hol WG, Verlinde CL, Merritt EA
J Mol Biol 381 975-88 (2008)
PMID: 18602399

Function and Biology Details

Reactions catalysed: 
S-methyl-5'-thioadenosine + H(2)O = S-methyl-5'-thioinosine + NH(3)
2'-deoxyadenosine + H(2)O = 2'-deoxyinosine + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107702 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Adenosine deaminase Chain: A
Molecule details ›
Chain: A
Length: 371 amino acids
Theoretical weight: 43.48 KDa
Source organism: Plasmodium vivax
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A5KE01 (Residues: 1-363; Coverage: 100%)
Gene names: ADA, PVX_111245
Sequence domains: Adenosine deaminase
Structure domains: Metal-dependent hydrolases

Ligands and Environments

3 bound ligands:
Ligand ZN 1 x ZN
Ligand ADN 1 x ADN
Ligand CCN 2 x CCN
1 modified residue:
Ligand MSE 11 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: C2221
Unit cell:
a: 143.962Å b: 146.608Å c: 50.398Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.157 0.201
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

4 review citations

New medicines to improve control and contribute to the eradication of malaria.
Wells et al. (2009)
3 more

6 mentions without citation

Structural basis for the growth factor activity of human adenosine deaminase ADA2.
Zavialov et al. (2010)
5 more