1ybv Summary

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STRUCTURE OF TRIHYDROXYNAPHTHALENE REDUCTASE IN COMPLEX WITH NADPH AND AN ACTIVE SITE INHIBITOR

The structure was published by Andersson, A., Jordan, D., Schneider, G., and Lindqvist, Y., in 1996 in a paper entitled "Crystal structure of the ternary complex of 1,3,8-trihydroxynaphthalene reductase from Magnaporthe grisea with NADPH and an active-site inhibitor." (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.8 Å and deposited in 1996.

The experimental data on which the structure is based was also deposited.

This PDB entry contains multiple copies of the structure of TRIHYDROXYNAPHTHALENE REDUCTASE.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule most likely forms homotetramers.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):


Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A TRIHYDROXYNAPHTHALENE REDUCTASE Q12634 (1-283) (T4HR_MAGO7)search Magnaporthe oryzae 70-15search 100% 283 95%
B TRIHYDROXYNAPHTHALENE REDUCTASE Q12634 (1-283) (T4HR_MAGO7)search Magnaporthe oryzae 70-15search 100% 283 95%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
Q12634 (1 - 283) TRIHYDROXYNAPHTHALENE REDUCTASE Magnaporthe grisea

Chain Structural classification (SCOP) Structural classification (CATH) Sequence family (Pfam)
A, B (Q12634) Tyrosine-dependent oxidoreductasessearch NAD(P)-binding Rossmann-like Domainsearch PF00106: short chain dehydrogenasesearch

Chain ID Cellular component (GO) Molecular function (GO) Biological process (GO)
A, B (Q12634) cellular_componentsearch tetrahydroxynaphthalene reductase activitysearch oxidoreductase activitysearch metabolic processsearch melanin biosynthetic processsearch oxidation-reduction processsearch

Chain InterPro annotation
A, B Short-chain dehydrogenase/reductase SDRsearch Glucose/ribitol dehydrogenasesearch NAD(P)-binding domainsearch Short-chain dehydrogenase/reductase, conserved sitesearch