1G0O

STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND PYROQUILON

Summary for 1G0O

• Entry DOI: 10.2210/pdb1g0o/pdb
• Related: 1DOH 1G0N 1YBV
• Descriptor: TRIHYDROXYNAPHTHALENE REDUCTASE, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, PYROQUILON, ... (4 entities in total)
• Functional Keywords: protein-nadph-active site inhibitor complex, dinucleotide binding fold, oxidoreductase, short chain dehydrogenase, oxidoreductase-oxidoreductase inhibitor complex, oxidoreductase/oxidoreductase inhibitor
• Biological source: Magnaporthe grisea
• Total number of polymer chains: 4
• Total formula weight: 124385.26

Authors

Liao, D.,Basarab, G.S.,Gatenby, A.A.,Valent, B.,Jordan, D.B. (deposition date: 2000-10-06, release date: 2001-06-06, Last modification date: 2024-02-07)

Primary citation

Liao, D.,Basarab, G.S.,Gatenby, A.A.,Valent, B.,Jordan, D.B.
Structures of trihydroxynaphthalene reductase-fungicide complexes: implications for structure-based design and catalysis.
Structure, 9:19-28, 2001

PubMed Abstract: Trihydroxynaphthalene reductase catalyzes two intermediate steps in the fungal melanin biosynthetic pathway. The enzyme, a typical short-chain dehydrogenase, is the biochemical target of three commercial fungicides. The fungicides bind preferentially to the NADPH form of the enzyme.

PubMed: 11342131
DOI: 10.1016/S0969-2126(00)00548-7

Experimental method

X-RAY DIFFRACTION (1.7 Å)