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1qj4
From Proteopedia
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(New page: 200px<br /> <applet load="1qj4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qj4, resolution 1.10Å" /> '''HYDROXYNITRILE-LYAS...)
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Revision as of 17:19, 29 October 2007
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HYDROXYNITRILE-LYASE FROM HEVEA BRASILIENSIS AT ATOMIC RESOLUTION
Overview
The X-ray crystal structure of native hydroxynitrile lyase from Hevea, brasiliensis (Hb-HNL) has been determined at 1.1 A resolution. It refined, to a final R of 11.5% for all data and an Rfree of 14.4%. The favorable, data-to-parameter ratio at atomic resolution made the refinement of, individual anisotropic displacement parameters possible. The data also, allowed a clear distinction of the alternate orientations of all histidine, and the majority of asparagine and glutamine side chains. A number of, hydrogen atoms, including one on the imidazole of the mechanistically, important His-235, became visible as peaks in a difference electron, density map. The structure revealed a discretely disordered sidechain of, Ser-80, which is part of the putative catalytic triad. Analysis of the, ... [(full description)]
About this Structure
1QJ4 is a [Single protein] structure of sequence from [Hevea brasiliensis] with SO4 and GOL as [ligands]. Active as [[1]], with EC number [4.2.1.39]. Full crystallographic information is available from [OCA].
Reference
Atomic resolution crystal structure of hydroxynitrile lyase from Hevea brasiliensis., Gruber K, Gugganig M, Wagner UG, Kratky C, Biol Chem. 1999 Jul-Aug;380(7-8):993-1000. PMID:10494852
Page seeded by OCA on Mon Oct 29 19:24:12 2007
