5KXU
Structure Proteinase K determined by SACLA
Summary for 5KXU
| Entry DOI | 10.2210/pdb5kxu/pdb |
| Related | 5KXV |
| Descriptor | Proteinase K, CALCIUM ION, NITRATE ION, ... (4 entities in total) |
| Functional Keywords | serine protease, hydrolysis, aminolysis, catalytic triad, hydrolase |
| Biological source | Engyodontium album |
| Total number of polymer chains | 1 |
| Total formula weight | 29100.95 |
| Authors | Masuda, T.,Suzuki, M.,Inoue, S.,Numata, K.,Sugahara, M. (deposition date: 2016-07-20, release date: 2017-06-07, Last modification date: 2024-10-23) |
| Primary citation | Masuda, T.,Suzuki, M.,Inoue, S.,Song, C.,Nakane, T.,Nango, E.,Tanaka, R.,Tono, K.,Joti, Y.,Kameshima, T.,Hatsui, T.,Yabashi, M.,Mikami, B.,Nureki, O.,Numata, K.,Iwata, S.,Sugahara, M. Atomic resolution structure of serine protease proteinase K at ambient temperature. Sci Rep, 7:45604-45604, 2017 Cited by PubMed Abstract: Atomic resolution structures (beyond 1.20 Å) at ambient temperature, which is usually hampered by the radiation damage in synchrotron X-ray crystallography (SRX), will add to our understanding of the structure-function relationships of enzymes. Serial femtosecond crystallography (SFX) has attracted surging interest by providing a route to bypass such challenges. Yet the progress on atomic resolution analysis with SFX has been rather slow. In this report, we describe the 1.20 Å resolution structure of proteinase K using 13 keV photon energy. Hydrogen atoms, water molecules, and a number of alternative side-chain conformations have been resolved. The increase in the value of B-factor in SFX suggests that the residues and water molecules adjacent to active sites were flexible and exhibited dynamic motions at specific substrate-recognition sites. PubMed: 28361898DOI: 10.1038/srep45604 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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