1klt
From Proteopedia
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CRYSTAL STRUCTURE OF PMSF-TREATED HUMAN CHYMASE AT 1.9 ANGSTROMS RESOLUTION
Overview
The X-ray crystal structure of human chymase has been determined to 1.9 A, resolution using molecular replacement methods. This first structure of, human chymase is present as the Ser 195 ester of alpha-toluenesulfonic, acid. The refined structure (Rcryst = 0.183) shows that the inhibitor, phenyl moiety lies at the top of the major specificity pocket, S1, while, the sulfur is covalently linked to Ser 195-O gamma. The sulfonyl oxygens, interact with the oxyanion hole and with His 57-N delta 1. The presence of, the inhibitor disturbs the usual gauche position of His 57 and forces it, to the trans conformer. Though the primary binding pockets are similarly, specific in chymase and chymotrypsin, examination of the extended, substrate binding sites reveals the structural basis for chymase's ... [(full description)]
About this Structure
1KLT is a [Single protein] structure of sequence from [Homo sapiens] with PMS as [ligand]. Active as [[1]], with EC number [3.4.21.39]. Full crystallographic information is available from [OCA].
Reference
Crystal structure of phenylmethanesulfonyl fluoride-treated human chymase at 1.9 A., McGrath ME, Mirzadegan T, Schmidt BF, Biochemistry. 1997 Nov 25;36(47):14318-24. PMID:9400368
Page seeded by OCA on Mon Oct 29 21:36:36 2007
