› 1pn9

X-ray diffraction
2Å resolution

Crystal structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae

Released:
DOI: 10.2210/pdb1pn9/pdb
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Source organism: Anopheles gambiae
Primary publication:
Structure of an insect delta-class glutathione S-transferase from a DDT-resistant strain of the malaria vector Anopheles gambiae.
Chen L, Hall PR, Zhou XE, Ranson H, Hemingway J, Meehan EJ
Acta Crystallogr D Biol Crystallogr 59 2211-7 (2003)
PMID: 14646079

Function and Biology Details

Reactions catalysed: 
RX + glutathione = HX + R-S-glutathione
1,1,1-trichloro-2,2-bis(4-chlorophenyl)ethane = 1,1-dichloro-2,2-bis(4-chlorophenyl)ethylene + chloride
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187995 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutathione S-transferase 1, isoform D Chains: A, B
Molecule details ›
Chains: A, B
Length: 209 amino acids
Theoretical weight: 23.47 KDa
Source organism: Anopheles gambiae
Expression system: Escherichia coli
UniProt:
  • Canonical: Q93113 (Residues: 1-209; Coverage: 100%)
Gene names: AGAP004164, GST1a, GstD1
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GTX 2 x GTX
No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: P212121
Unit cell:
a: 50.2Å b: 89.4Å c: 100Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.209 0.209 0.254
Expression system: Escherichia coli

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Citations

1 review citation

Insect glutathione transferases.
Ketterman et al. (2011)
30 other articles

12 mentions without citation

Glutathione transferases are structural and functional outliers in the thioredoxin fold.
Atkinson et al. (2009)
11 more

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