1qnj
From Proteopedia
(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...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1qnj.jpg|left|200px]]<br /><applet load="1qnj" size=" | + | [[Image:1qnj.jpg|left|200px]]<br /><applet load="1qnj" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1qnj, resolution 1.10Å" /> | caption="1qnj, resolution 1.10Å" /> | ||
'''THE STRUCTURE OF NATIVE PORCINE PANCREATIC ELASTASE AT ATOMIC RESOLUTION (1.1 A)'''<br /> | '''THE STRUCTURE OF NATIVE PORCINE PANCREATIC ELASTASE AT ATOMIC RESOLUTION (1.1 A)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | A data set from the serine protease porcine pancreatic elastase was | + | 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== | ==About this Structure== | ||
| - | 1QNJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with NA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] Full crystallographic information is available from [http:// | + | 1QNJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QNJ OCA]. |
==Reference== | ==Reference== | ||
| Line 23: | Line 23: | ||
[[Category: hydrolase(serine protease)]] | [[Category: hydrolase(serine protease)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:41:40 2008'' |
Revision as of 12:41, 21 February 2008
|
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 and 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
Page seeded by OCA on Thu Feb 21 14:41:40 2008
