1qj4
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The X-ray crystal structure of native hydroxynitrile lyase from Hevea | + | 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 anisotropy indicated an increased mobility of residues near the entrance to the active site and within the active site. |
==About this Structure== | ==About this Structure== | ||
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[[Category: oxynitrilase]] | [[Category: oxynitrilase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:40:10 2008'' |
Revision as of 12:40, 21 February 2008
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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 anisotropy indicated an increased mobility of residues near the entrance to the active site and within the active site.
About this Structure
1QJ4 is a Single protein structure of sequence from Hevea brasiliensis with and as ligands. Active as Gluconate dehydratase, with EC number 4.2.1.39 Known structural/functional Site: . 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
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