3GDN
Almond hydroxynitrile lyase in complex with benzaldehyde
Summary for 3GDN
Entry DOI | 10.2210/pdb3gdn/pdb |
Related | 1ju2 3GDP |
Descriptor | R-oxynitrile lyase isoenzyme 1, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-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 | 118630.51 |
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 Cited by PubMed: 19256550DOI: 10.1021/bi802162s PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.67 Å) |
Structure validation
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