3GDP

Hydroxynitrile lyase from almond, monoclinic crystal form

Summary for 3GDP

• Entry DOI: 10.2210/pdb3gdp/pdb
• Related: 1ju2 3gdn
• Descriptor: R-oxynitrile lyase isoenzyme 1, alpha-D-mannopyranose-(1-6)-alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-[beta-L-fucopyranose-(1-3)]2-acetamido-2-deoxy-beta-D-glucopyranose, alpha-L-fucopyranose-(1-3)-[2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)]2-acetamido-2-deoxy-beta-D-glucopyranose, ... (10 entities in total)
• Functional Keywords: hydroxynitrile lyase, flavin, gmc oxidoreductase, almond, cyanogenesis, flavoprotein, lyase
• Biological source: Prunus dulcis (sweet almond)
• Total number of polymer chains: 2
• Total formula weight: 118756.56

Authors

Dreveny, I.,Gruber, K.,Kratky, C. (deposition date: 2009-02-24, release date: 2009-03-24, Last modification date: 2023-09-06)

• Primary citation: Dreveny, I.,Andryushkova, A.S.,Glieder, A.,Gruber, K.,Kratky, C.; Substrate binding in the FAD-dependent hydroxynitrile lyase from almond provides insight into the mechanism of cyanohydrin formation and explains the absence of dehydrogenation activity.; Biochemistry, 48:3370-3377, 2009; PubMed: 19256550; DOI: 10.1021/bi802162s

Experimental method

X-RAY DIFFRACTION (1.57 Å)