1AHA
THE N-GLYCOSIDASE MECHANISM OF RIBOSOME-INACTIVATING PROTEINS IMPLIED BY CRYSTAL STRUCTURES OF ALPHA-MOMORCHARIN
Summary for 1AHA
Entry DOI | 10.2210/pdb1aha/pdb |
Descriptor | ALPHA-MOMORCHARIN, ADENINE (3 entities in total) |
Functional Keywords | glycosidase |
Biological source | Momordica charantia (balsam pear) |
Total number of polymer chains | 1 |
Total formula weight | 27531.41 |
Authors | Ren, J.,Wang, Y.,Dong, Y.,Stuart, D.I. (deposition date: 1994-01-07, release date: 1994-06-22, Last modification date: 2024-02-07) |
Primary citation | Ren, J.,Wang, Y.,Dong, Y.,Stuart, D.I. The N-glycosidase mechanism of ribosome-inactivating proteins implied by crystal structures of alpha-momorcharin. Structure, 2:7-16, 1994 Cited by PubMed Abstract: alpha-Momorcharin (alpha MMC) is a type I ribosome-inactivating protein. It inhibits protein synthesis by hydrolytically removing a specific adenine residue from a highly conserved, single-stranded loop of rRNA. PubMed: 8075985DOI: 10.1016/S0969-2126(00)00004-6 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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