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PDBe Entry: 1ads
AN UNLIKELY SUGAR SUBSTRATE SITE IN THE 1.65 ANGSTROMS STRUCTURE OF THE HUMAN ALDOSE REDUCTASE HOLOENZYME IMPLICATED IN DIABETIC COMPLICATIONS
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| Summary |  |
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| Header |
OXIDOREDUCTASE
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| Method | X-RAY DIFFRACTION | |||||||||||||
| Experiment | Resolution: 1.65 Å, R-factor: 20.0%, Spacegroup: P 21 21 21 | |||||||||||||
| Released | 31/10/1993, deposition: 08/07/1992, last revision: 24/02/2009 | |||||||||||||
| Authors |
Wilson, D.K.; Quiocho, F.A.
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| Primary citation |
An unlikely sugar substrate site in the 1.65 A structure of the human aldose reductase holoenzyme implicated in diabetic complications. SCIENCE vol:257, pag:81-84 (1992) [PubMed ID 1621098 ]
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| Keywords |
OXIDOREDUCTASE
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| EC |
1.1.1.21 ExPASy BRENDA (A)
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| Organism |
Homo sapiens(human) 9606(A)
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| UniProt |
Aldose reductase (EC 1.1.1.21) (AR) (Aldehyde reductase) P15121 (A)
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| Solvent | A | |||||||||||||
| Polymers |
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| Heterogens |
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