1pif
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(New page: 200px<br /> <applet load="1pif" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pif, resolution 2.3Å" /> '''PIG ALPHA-AMYLASE'''...)
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Revision as of 19:03, 29 October 2007
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PIG ALPHA-AMYLASE
Overview
The crystal structures of porcine pancreatic alpha-amylase isozyme II (PPA, II) in its free form and complexed with the trestatin A derived, pseudo-octasaccharide V-1532 have been determined using Patterson search, techniques at resolutions of 2.3 and 2.2 angstroms, respectively. Seven, rings of the competitive inhibitor V-1532 could be detected in the active, site region as well as two maltose units in secondary binding sites on the, surface. V-1532 occupies the five central sugar binding subsites similar, to the PPA/acarbose structure. A sixth ring exists at the reducing end, connecting two symmetry related PPA molecules. The seventh moiety, a, 6-hydroxymethylconduritol ring, is located at the non-reducing end. The, electron density for this ring is relatively weak, indicating ... [(full description)]
About this Structure
1PIF is a [Single protein] structure of sequence from [Sus scrofa] with CA and CL as [ligands]. Active as [[1]], with EC number [3.2.1.1]. Full crystallographic information is available from [OCA].
Reference
Carbohydrate and protein-based inhibitors of porcine pancreatic alpha-amylase: structure analysis and comparison of their binding characteristics., Machius M, Vertesy L, Huber R, Wiegand G, J Mol Biol. 1996 Jul 19;260(3):409-21. PMID:8757803
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