Atomic resolution structure of native porcine pancreatic elastase at 1.1 A.
A data set from the serine protease porcine pancreatic elastase was collected at atomic resolution (1.1 A) with synchrotron radiation. The improved resolution allows the determination of atom positions with high accuracy, as well as the localization of H atoms. Three residues could be modelled in alternative positions. The catalytic triad of elastase consists of His57, Asp102 and Ser195. The His57 N(delta1) H atom was located at a distance of 0.82 A from the N(delta1) atom. The distance between His57 N(delta1) and Asp102 O(delta2) is 2.70 +/- 0.04 A, thus indicating normal hydrogen-bonding geometry. Additional H atoms at His57 N(varepsilon2) and Ser195 O(gamma) could not be identified in the F(o) - F(c) density maps.
Würtele
M
M
Institut für Biochemie der Charité, Humboldt-Universität zu Berlin, Monbijoustrasse 2, D-10117 Berlin, Germany.
Hahn
M
M
Hilpert
K
K
Höhne
W
W
D000818:Animals; D020134:Catalytic Domain; D003198:Computer Simulation; D018360:Crystallography, X-Ray / Q000379:methods; D006639:Histidine; D008958:Models, Molecular; D010196:Pancreatic Elastase / Q000737:chemistry*; D011487:Protein Conformation; D012694:Serine; D013552:Swine; D017356:Synchrotrons
D012694:Serine; D006639:Histidine; D010196:Pancreatic Elastase