1QNJ

THE STRUCTURE OF NATIVE PORCINE PANCREATIC ELASTASE AT ATOMIC RESOLUTION (1.1 A)

Summary for 1QNJ

• Entry DOI: 10.2210/pdb1qnj/pdb
• Related: 1B0E 1BMA 1BTU 1EAI 1EAS 1EAT 1EAU 1ELA 1ELB 1ELC 1ELD 1ELE 1ELF 1ELG 1ESA 1ESB 1EST 1INC 1JIM 1LVY 1NES 2EST 3EST 4EST 5EST 6EST 7EST 8EST 9EST
• Descriptor: ELASTASE, SODIUM ION, SULFATE ION, ... (4 entities in total)
• Functional Keywords: hydrolase (serine protease), hydrolase(serine protease), atomic resolution
• Biological source: SUS SCROFA (PIG)
• Total number of polymer chains: 1
• Total formula weight: 26144.13

Authors

Wurtele, M.,Hahn, M.,Hilpert, K.,Hohne, W. (deposition date: 1999-10-15, release date: 2000-03-31, Last modification date: 2023-12-13)

Primary citation

Wurtele, M.,Hahn, M.,Hilpert, K.,Hohne, W.
Atomic Resolution Structure of Native Porcine Pancreatic Elastase at 1.1 A
Acta Crystallogr.,Sect.D, 56:520-, 2000

PubMed Abstract: 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.

PubMed: 10739939
DOI: 10.1107/S0907444900000299

Experimental method

X-RAY DIFFRACTION (1.1 Å)