6Y5T

Crystal structure of savinase at room temperature

Summary for 6Y5T

Entry DOI	10.2210/pdb6y5t/pdb
Descriptor	Subtilisin Savinase, CALCIUM ION, SODIUM ION, ... (4 entities in total)
Functional Keywords	subtilisin savinase, protein dynamics, alternative conformations, hydrolase
Biological source	Bacillus lentus
Total number of polymer chains	1
Total formula weight	26781.45
Authors	Wu, S.,Moroz, O.,Turkenburg, J.,Nielsen, J.E.,Wilson, K.S.,Teilum, K. (deposition date: 2020-02-25, release date: 2020-06-17, Last modification date: 2024-01-24)
Primary citation	Wu, S.,Nguyen, T.T.T.N.,Moroz, O.V.,Turkenburg, J.P.,Nielsen, J.E.,Wilson, K.S.,Rand, K.D.,Teilum, K. Conformational heterogeneity of Savinase from NMR, HDX-MS and X-ray diffraction analysis. Peerj, 8:e9408-e9408, 2020 Cited by PubMed Abstract: Several examples have emerged of enzymes where slow conformational changes are of key importance for function and where low populated conformations in the resting enzyme resemble the conformations of intermediate states in the catalytic process. Previous work on the subtilisin protease, Savinase, from by NMR spectroscopy suggested that this enzyme undergoes slow conformational dynamics around the substrate binding site. However, the functional importance of such dynamics is unknown. PubMed: 32617193 DOI: 10.7717/peerj.9408 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.1 Å)

Structure validation