Structural highlights
Function
CELA1_PIG Acts upon elastin.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Wurtele M, Hahn M, Hilpert K, Hohne W. Atomic resolution structure of native porcine pancreatic elastase at 1.1 A. Acta Crystallogr D Biol Crystallogr. 2000 Apr;56(Pt 4):520-3. PMID:10739939
