Summary for 4YTA
| Entry DOI | 10.2210/pdb4yta/pdb |
| Descriptor | Cationic trypsin, GLYCEROL, SULFATE ION, ... (6 entities in total) |
| Functional Keywords | serine protease, hydrolase |
| Biological source | Bos taurus (cattle) |
| Cellular location | Secreted, extracellular space: P00760 |
| Total number of polymer chains | 1 |
| Total formula weight | 24621.40 |
| Authors | Fisher, S.J.,Helliwell, J.R.,Blakeley, M.P.,Cianci, M.,McSweeny, S. (deposition date: 2015-03-17, release date: 2015-05-27, Last modification date: 2024-10-16) |
| Primary citation | Fisher, S.J.,Blakeley, M.P.,Cianci, M.,McSweeney, S.,Helliwell, J.R. Protonation-state determination in proteins using high-resolution X-ray crystallography: effects of resolution and completeness. Acta Crystallogr. D Biol. Crystallogr., 68:800-809, 2012 Cited by PubMed Abstract: A bond-distance analysis has been undertaken to determine the protonation states of ionizable amino acids in trypsin, subtilisin and lysozyme. The diffraction resolutions were 1.2 Å for trypsin (97% complete, 12% H-atom visibility at 2.5σ), 1.26 Å for subtilisin (100% complete, 11% H-atom visibility at 2.5σ) and 0.65 Å for lysozyme (PDB entry 2vb1; 98% complete, 30% H-atom visibility at 3σ). These studies provide a wide diffraction resolution range for assessment. The bond-length e.s.d.s obtained are as small as 0.008 Å and thus provide an exceptional opportunity for bond-length analyses. The results indicate that useful information can be obtained from diffraction data at around 1.2-1.3 Å resolution and that minor increases in resolution can have significant effects on reducing the associated bond-length standard deviations. The protonation states in histidine residues were also considered; however, owing to the smaller differences between the protonated and deprotonated forms it is much more difficult to infer the protonation states of these residues. Not even the 0.65 Å resolution lysozyme structure provided the necessary accuracy to determine the protonation states of histidine. PubMed: 22751665DOI: 10.1107/S0907444912012589 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.2 Å) |
Structure validation
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