1CYD

CARBONYL REDUCTASE COMPLEXED WITH NADPH AND 2-PROPANOL

Summary for 1CYD

• Entry DOI: 10.2210/pdb1cyd/pdb
• Descriptor: CARBONYL REDUCTASE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, ISOPROPYL ALCOHOL, ... (4 entities in total)
• Functional Keywords: short-chain dehydrogenase, oxidoreductase
• Biological source: Mus musculus (house mouse)
• Cellular location: Mitochondrion matrix: P08074
• Total number of polymer chains: 4
• Total formula weight: 107178.78

Authors

Tanaka, N.,Nonaka, T.,Mitsui, Y. (deposition date: 1995-09-01, release date: 1996-10-14, Last modification date: 2024-02-07)

Primary citation

Tanaka, N.,Nonaka, T.,Nakanishi, M.,Deyashiki, Y.,Hara, A.,Mitsui, Y.
Crystal structure of the ternary complex of mouse lung carbonyl reductase at 1.8 A resolution: the structural origin of coenzyme specificity in the short-chain dehydrogenase/reductase family.
Structure, 4:33-45, 1996

PubMed Abstract: Mouse lung carbonyl reductase (MLCR) is a member of the short-chain dehydrogenase/reductase (SDR) family. Although it uses both NADPH and NADH as coenzymes, the structural basis of its strong preference for NADPH is unknown.

PubMed: 8805511
DOI: 10.1016/S0969-2126(96)00007-X

Experimental method

X-RAY DIFFRACTION (1.8 Å)