Summary for 2Q33
| Entry DOI | 10.2210/pdb2q33/pdb |
| Descriptor | D-MONELLIN CHAIN A, D-MONELLIN CHAIN B (3 entities in total) |
| Functional Keywords | alpha/beta, all-d protein, de novo protein |
| Total number of polymer chains | 2 |
| Total formula weight | 10692.17 |
| Authors | Hung, L.-W.,Kohmura, M.,Ariyoshi, Y.,Kim, S.-H. (deposition date: 2007-05-29, release date: 2007-11-13, Last modification date: 2024-11-20) |
| Primary citation | Hung, L.-W.,Kohmura, M.,Ariyoshi, Y.,Kim, S.-H. Structure of an Enantiomeric Protein, D-Monellin at 1.8 A Resolution. Acta Crystallogr.,Sect.D, 54:494-500, 1998 Cited by PubMed Abstract: The D-enantiomer of a potently sweet protein, monellin, has been crystallized and analyzed by X-ray crystallography at 1.8 A resolut ion. Two crystal forms (I and II) appeared under crystallization conditions similar, but not identical, to the crystallization conditions of natural L-monellin. There are four molecules per asymmetric unit in crystal form I and one in crystal form II. Crystal form I is not reproducible and is equivalent to that of monoclinic L-monellin. Intermonomer contacts in crystal form II are very different from those found in natural L-monellin crystals. The backbone trace of D-monellin resembles very closely the mirror image of that of L-monellin, but the N- and C-terminus backbones as well as several side-chain conformations of D-monellin are different from those of natural L-monellin. Most of these apparent differences may be attributable to the crystal packing differences. PubMed: 9867435DOI: 10.1107/S0907444997012225 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
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