 |
PDBsum entry 1guh
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
|
|
Key reference
|
|
|
Title
|
|
Structure determination and refinement of human alpha class glutathione transferase a1-1, And a comparison with the mu and pi class enzymes.
|
|
|
Authors
|
|
I.Sinning,
G.J.Kleywegt,
S.W.Cowan,
P.Reinemer,
H.W.Dirr,
R.Huber,
G.L.Gilliland,
R.N.Armstrong,
X.Ji,
P.G.Board.
|
|
|
Ref.
|
|
J Mol Biol, 1993,
232,
192-212.
|
|
|
PubMed id
|
|
|
|
|
|
Abstract
|
|
|
The crystal structure of human alpha class glutathione transferase A1-1 has been
determined and refined to a resolution of 2.6 A. There are two copies of the
dimeric enzyme in the asymmetric unit. Each monomer is built from two domains. A
bound inhibitor, S-benzyl-glutathione, is primarily associated with one of these
domains via a network of hydrogen bonds and salt-links. In particular, the
sulphur atom of the inhibitor forms a hydrogen bond to the hydroxyl group of
Tyr9 and the guanido group of Arg15. The benzyl group of the inhibitor is
completely buried in a hydrophobic pocket. The structure shows an overall
similarity to the mu and pi class enzymes particularly in the
glutathione-binding domain". The main difference concerns the extended C
terminus of the alpha class enzyme which forms an extra alpha-helix that blocks
one entrance to the active site and makes up part of the substrate binding site.
|
|
|
|
|
|
|
