1SC9
Hydroxynitrile Lyase from Hevea brasiliensis in complex with the natural substrate acetone cyanohydrin
Summary for 1SC9
| Entry DOI | 10.2210/pdb1sc9/pdb |
| Related | 1SCI 1SCK 1SCQ 1qj4 1yas 2yas 3yas 4yas 5yas 6yas 7yas |
| Descriptor | (S)-acetone-cyanohydrin lyase, SULFATE ION, 2-HYDROXY-2-METHYLPROPANENITRILE, ... (4 entities in total) |
| Functional Keywords | alpha-beta hydrolase fold, substrate complex, catalytic triad, lyase |
| Biological source | Hevea brasiliensis |
| Total number of polymer chains | 1 |
| Total formula weight | 29539.83 |
| Authors | Gruber, K.,Gartler, G.,Krammer, B.,Schwab, H.,Kratky, C. (deposition date: 2004-02-12, release date: 2004-06-29, Last modification date: 2023-10-25) |
| Primary citation | Gruber, K.,Gartler, G.,Krammer, B.,Schwab, H.,Kratky, C. Reaction mechanism of hydroxynitrile lyases of the alpha/beta-hydrolase superfamily: the three-dimensional structure of the transient enzyme-substrate complex certifies the crucial role of LYS236 J.Biol.Chem., 279:20501-20510, 2004 Cited by PubMed: 14998991DOI: 10.1074/jbc.M401575200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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