1EE2

THE STRUCTURE OF STEROID-ACTIVE ALCOHOL DEHYDROGENASE AT 1.54 A RESOLUTION

Summary for 1EE2

• Entry DOI: 10.2210/pdb1ee2/pdb
• Related: 2OHX
• Descriptor: ALCOHOL DEHYDROGENASE, ZINC ION, NICOTINAMIDE-ADENINE-DINUCLEOTIDE, ... (5 entities in total)
• Functional Keywords: dehydrogenase, alcohol, nicotinamide coenzyme, steroid binding, oxidoreductase
• Biological source: Equus caballus (horse)
• Cellular location: Cytoplasm: P00328
• Total number of polymer chains: 2
• Total formula weight: 81487.81

Authors

Adolph, H.W. (deposition date: 2000-01-30, release date: 2000-10-27, Last modification date: 2024-02-07)

• Primary citation: Adolph, H.W.,Zwart, P.,Meijers, R.,Hubatsch, I.,Kiefer, M.,Lamzin, V.,Cedergren-Zeppezauer, E.; Structural basis for substrate specificity differences of horse liver alcohol dehydrogenase isozymes.; Biochemistry, 39:12885-12897, 2000; PubMed: 11041853; DOI: 10.1021/bi001376s

Experimental method

X-RAY DIFFRACTION (1.54 Å)