1gsf: Difference between revisions
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|PDB= 1gsf |SIZE=350|CAPTION= <scene name='initialview01'>1gsf</scene>, resolution 2.7Å | |PDB= 1gsf |SIZE=350|CAPTION= <scene name='initialview01'>1gsf</scene>, resolution 2.7Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=EAA:ETHACRYNIC ACID'>EAA</scene> | |LIGAND= <scene name='pdbligand=EAA:ETHACRYNIC+ACID'>EAA</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glutathione_transferase Glutathione transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.18 2.5.1.18] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1gsf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1gsf OCA], [http://www.ebi.ac.uk/pdbsum/1gsf PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1gsf RCSB]</span> | |||
}} | }} | ||
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[[Category: Jones, T A.]] | [[Category: Jones, T A.]] | ||
[[Category: Sinning, I.]] | [[Category: Sinning, I.]] | ||
[[Category: a1-1]] | [[Category: a1-1]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:50:38 2008'' | ||
Revision as of 17:50, 30 March 2008
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| 1gsf, resolution 2.7Å | |||||||||||||
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| Ligands: | EAA | ||||||||||||
| Activity: | Glutathione transferase, with EC number 2.5.1.18 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
GLUTATHIONE TRANSFERASE A1-1 COMPLEXED WITH ETHACRYNIC ACID
Overview
BACKGROUND: Glutathione transferases (GSTs) constitute a family of isoenzymes that catalyze the conjugation of the tripeptide glutathione with a wide variety of hydrophobic compounds bearing an electrophilic functional group. Recently, a number of X-ray structures have been reported which have defined both the glutathione- and the substrate-binding sites in these enzymes. The structure of the glutathione-free enzyme from a mammalian source has not, however, been reported previously. RESULTS: We have solved structures of a human alpha-class GST, isoenzyme A1-1, both in the unliganded form and in complexes with the inhibitor ethacrynic acid and its glutathione conjugate. These structures have been refined to resolutions of 2.5 A, 2.7 A and 2.0 A respectively. Both forms of the inhibitor are clearly present in the associated electron density. CONCLUSIONS: The major differences among the three structures reported here involve the C-terminal alpha-helix, which is a characteristic of the alpha-class enzyme. This helix forms a lid over the active site when the hydrophobic substrate binding site (H-site) is occupied but it is otherwise disordered. Ethacrynic acid appears to bind in a non-productive mode in the absence of the coenzyme glutathione.
About this Structure
1GSF is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural analysis of human alpha-class glutathione transferase A1-1 in the apo-form and in complexes with ethacrynic acid and its glutathione conjugate., Cameron AD, Sinning I, L'Hermite G, Olin B, Board PG, Mannervik B, Jones TA, Structure. 1995 Jul 15;3(7):717-27. PMID:8591048
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