4gr1 | pdb_00004gr1
THE BINDING OF THE RETRO-ANALOGUE OF GLUTATHIONE DISULFIDE TO GLUTATHIONE REDUCTASE
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| 4gr1, resolution 2.4Å | |||||||||||||
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| Ligands: | FAD, PO4, RGS | ||||||||||||
| Activity: | Glutathione-disulfide reductase, with EC number 1.8.1.7 | ||||||||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Overview
The retro-analogue of glutathione disulfide was bound to the GSSG binding site of crystalline glutathione reductase. The binding mode revealed why the analogue is a very poor substrate in enzyme catalysis. The observed binding mode difference between natural substrate and retro-analogue is explained.
About this Structure
4GR1 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The binding of the retro-analogue of glutathione disulfide to glutathione reductase., Janes W, Schulz GE, J Biol Chem. 1990 Jun 25;265(18):10443-5. PMID:2355009
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