2uu8
From Proteopedia
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X-RAY STRUCTURE OF NI, CA CONCANAVALIN A AT ULTRA-HIGH RESOLUTION (0.94A)
Overview
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 Structure
2UU8 is a [Single protein] structure of sequence from [[1]] with NI and CA as [ligands]. Full crystallographic information is available from [OCA].
Reference
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
Page seeded by OCA on Mon Oct 29 17:51:35 2007
Categories: Single protein | Ahmed, H.U. | Blakeley, M.P. | Cianci, M. | Cruickshank, D.W.J. | Helliwell, J.R. | Hubbard, J.A. | CA | NI | Calcium | Jack bean | Lectin | Manganese | Metal-binding | Ni concanavalin a
