1qnj
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(New page: 200px<br /><applet load="1qnj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qnj, resolution 1.10Å" /> '''THE STRUCTURE OF NAT...)
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Revision as of 22:42, 20 November 2007
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THE STRUCTURE OF NATIVE PORCINE PANCREATIC ELASTASE AT ATOMIC RESOLUTION (1.1 A)
Overview
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.
About this Structure
1QNJ is a Single protein structure of sequence from Sus scrofa with NA and SO4 as ligands. Active as Pancreatic elastase, with EC number 3.4.21.36 Full crystallographic information is available from OCA.
Reference
Atomic resolution structure of native porcine pancreatic elastase at 1.1 A., Wurtele M, Hahn M, Hilpert K, Hohne W, Acta Crystallogr D Biol Crystallogr. 2000 Apr;56(Pt 4):520-3. PMID:10739939
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