1elt

STRUCTURE OF NATIVE PANCREATIC ELASTASE FROM NORTH ATLANTIC SALMON AT 1.61 ANGSTROMS RESOLUTION

spinqualitylabelsall models 1elt, resolution 1.61Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1elt is a 1 chain structure with sequence from Salmo salar. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Activity: Pancreatic elastase, with EC number 3.4.21.36 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [ELA1_SALSA] 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 The crystal structure of native salmon pancreatic elastase (SPE) has been solved by molecular-replacement methods, and refined by conventional conjugate-gradient methods and simulated-annealing techniques. The final R value is 17.2% for 21 389 reflections between 8.0 and 1.61 A, and the corresponding free R value is 23.9%. The overall tertiary structure of SPE is remarkably similar to that of porcine pancreatic elastase I (PPE), to which it shows about 67% sequence identity. The primary structure of SPE is determined from the electron-density maps, and only about 15 side chains are somewhat uncertain. Interesting differences between SPE and PPE, are one sequence deletion assigned to position 186, the residue 192 at the entrance of the specificity pocket is substituted from a Gln in PPE to Asn in SPE, and one of the calcium ligands is different. Furthermore, electron density is missing in SPE for the last three residues of the C-terminal helix. A comparison of the present amino-acid sequence of SPE with other sequences available indicates that SPE belongs to the class 1 pancreatic elastases. Structure of native pancreatic elastase from North Atlantic salmon at 1.61 A resolution.,Berglund GI, Willassen NP, Hordvik A, Smalas AO Acta Crystallogr D Biol Crystallogr. 1995 Nov 1;51(Pt 6):925-37. PMID:15299762 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Elastase

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