5T3H
bovine trypsin soaked with selenourea for 5 min
Summary for 5T3H
| Entry DOI | 10.2210/pdb5t3h/pdb |
| Descriptor | Cationic trypsin, CALCIUM ION, BENZAMIDINE, ... (7 entities in total) |
| Functional Keywords | trypsin, selenourea, hydrolase |
| Biological source | Bos taurus (Bovine) |
| Cellular location | Secreted, extracellular space: P00760 |
| Total number of polymer chains | 1 |
| Total formula weight | 24998.90 |
| Authors | |
| Primary citation | Luo, Z. Selenourea: a convenient phasing vehicle for macromolecular X-ray crystal structures. Sci Rep, 6:37123-37123, 2016 Cited by PubMed Abstract: Majority of novel X-ray crystal structures of proteins are currently solved using the anomalous diffraction signal provided by selenium after incorporation of selenomethionine instead of natural methionine by genetic engineering methods. However, selenium can be inserted into protein crystals in the form of selenourea (SeC(NH)), by adding the crystalline powder of selenourea into mother liquor or cryo-solution with native crystals, in analogy to the classic procedure of heavy-atom derivatization. Selenourea is able to bind to reactive groups at the surface of macromolecules primarily through hydrogen bonds, where the selenium atom may serve as acceptor and amide groups as donors. Selenourea has different chemical properties than heavy-atom reagents and halide ions and provides a convenient way of phasing crystal structures of macromolecules. PubMed: 27841370DOI: 10.1038/srep37123 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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