2uuf: Difference between revisions

Revision as of 18:32, 30 October 2007

THROMBIN-HIRUGEN BINARY COMPLEX AT 1.26A RESOLUTION

OverviewOverview

The protonation states of aspartic acids and glutamic acids as well as, histidine are investigated in four X-ray cases: Ni,Ca concanavalin A at, 0.94 A, a thrombin-hirugen binary complex at 1.26 A resolution and two, thrombin-hirugen-inhibitor ternary complexes at 1.32 and 1.39 A, resolution. The truncation of the Ni,Ca concanavalin A data at various, test resolutions between 0.94 and 1.50 A provided a test comparator for, the ;unknown' thrombin-hirugen carboxylate bond lengths. The protonation, states of aspartic acids and glutamic acids can be determined (on the, basis of convincing evidence) even to the modest resolution of 1.20 A as, exemplified by our X-ray crystal structure refinements of Ni and Mn, concanavalin A and also as indicated in the 1.26 A structure of thrombin, both of ... [(full description)]

About this StructureAbout this Structure

2UUF is a [Protein complex] structure of sequences from [Homo sapiens] with NA and CA as [ligands]. Active as [Thrombin], with EC number [3.4.21.5]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

ReferenceReference

The determination of protonation states in proteins., Ahmed HU, Blakeley MP, Cianci M, Cruickshank DW, Hubbard JA, Helliwell JR, Acta Crystallogr D Biol Crystallogr. 2007 Aug;63(Pt 8):906-22. Epub 2007, Jul 17. PMID:17642517

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