1qj4

From Proteopedia

(Difference between revisions)

Revision as of 06:02, 28 April 2021

HYDROXYNITRILE-LYASE FROM HEVEA BRASILIENSIS AT ATOMIC RESOLUTION

Structural highlights

1qj4 is a 1 chain structure with sequence from Hevbr. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1yas
Gene:	HNL (HEVBR)
Activity:	Lyase, with EC number and 4.1.2.47 4.1.2.46 and 4.1.2.47
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HNL_HEVBR] Involved in cyanogenesis, the release of HCN from injured tissues. Decomposes a varieties of (R) or (S) cyanohydrins into HCN and the corresponding aldehydes and ketones. The natural substrate of this enzyme is (S)-acetone cyanohydrin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gruber K, Gugganig M, Wagner UG, Kratky C. Atomic resolution crystal structure of hydroxynitrile lyase from Hevea brasiliensis. Biol Chem. 1999 Jul-Aug;380(7-8):993-1000. PMID:10494852

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1qj4"

@@ Line 3: / Line 3: @@
 <StructureSection load='1qj4' size='340' side='right'caption='[[1qj4]], [[Resolution|resolution]] 1.10&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1qj4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Hevbr Hevbr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QJ4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1qj4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hevbr Hevbr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QJ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QJ4 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1yas|1yas]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1yas|1yas]]</div></td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HNL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3981 HEVBR])</td></tr>
+<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HNL ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3981 HEVBR])</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lyase Lyase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.46 and 4.1.2.47 4.1.2.46 and 4.1.2.47] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Lyase Lyase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.46 and 4.1.2.47 4.1.2.46 and 4.1.2.47] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qj4 OCA], [http://pdbe.org/1qj4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1qj4 RCSB], [http://www.ebi.ac.uk/pdbsum/1qj4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1qj4 ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qj4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qj4 OCA], [https://pdbe.org/1qj4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qj4 RCSB], [https://www.ebi.ac.uk/pdbsum/1qj4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qj4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HNL_HEVBR HNL_HEVBR]] Involved in cyanogenesis, the release of HCN from injured tissues. Decomposes a varieties of (R) or (S) cyanohydrins into HCN and the corresponding aldehydes and ketones. The natural substrate of this enzyme is (S)-acetone cyanohydrin.
+[[https://www.uniprot.org/uniprot/HNL_HEVBR HNL_HEVBR]] Involved in cyanogenesis, the release of HCN from injured tissues. Decomposes a varieties of (R) or (S) cyanohydrins into HCN and the corresponding aldehydes and ketones. The natural substrate of this enzyme is (S)-acetone cyanohydrin.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1qj4

From Proteopedia

Revision as of 06:02, 28 April 2021

HYDROXYNITRILE-LYASE FROM HEVEA BRASILIENSIS AT ATOMIC RESOLUTION

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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