2g4l

From Proteopedia

(Difference between revisions)

Revision as of 02:28, 11 September 2015

Anomalous substructure of hydroxynitrile lyase

Structural highlights

2g4l is a 1 chain structure with sequence from Hevea brasiliensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:
Related:	2g4h, 2g4i, 2g4j, 2g4k, 2g4m, 2g4n, 2g4o, 2g4p, 2g4q, 2g4r, 2g4s, 2g4t, 2g4u, 2g4v, 2g4w, 2g4x, 2g4y, 2g4z, 2g51, 2g52, 2g55
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

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

23 different crystal forms of 19 different biological macromolecules were examined with respect to their anomalously scattering substructures using diffraction data collected at a wavelength of 2.0 A (6.2 keV). In more than 90% of the cases the substructure was found to contain more than just the protein S atoms. The data presented suggest that chloride, sulfate, phosphate or metal ions from the buffer or even from the purification protocol are frequently bound to the protein molecule and that these ions are often overlooked, especially if they are not bound at full occupancy. Thus, in order to fully describe the macromolecule under study, it seems desirable that any structure determination be complemented with a long-wavelength data set.

On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths.,Mueller-Dieckmann C, Panjikar S, Schmidt A, Mueller S, Kuper J, Geerlof A, Wilmanns M, Singh RK, Tucker PA, Weiss MS Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):366-80. Epub 2007, Feb 21. PMID:17327674^[1]

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

References

↑ Mueller-Dieckmann C, Panjikar S, Schmidt A, Mueller S, Kuper J, Geerlof A, Wilmanns M, Singh RK, Tucker PA, Weiss MS. On the routine use of soft X-rays in macromolecular crystallography. Part IV. Efficient determination of anomalous substructures in biomacromolecules using longer X-ray wavelengths. Acta Crystallogr D Biol Crystallogr. 2007 Mar;63(Pt 3):366-80. Epub 2007, Feb 21. PMID:17327674 doi:http://dx.doi.org/10.1107/S0907444906055624

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/2g4l"

Categories: Hevea brasiliensis | Lyase | Mueller-Dieckmann, C | Weiss, M S | Anomalous substructure of hydroxynitrile lyase

@@ Line 6: / Line 6: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CME:S,S-(2-HYDROXYETHYL)THIOCYSTEINE'>CME</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2g4h|2g4h]], [[2g4i|2g4i]], [[2g4j|2g4j]], [[2g4k|2g4k]], [[2g4m|2g4m]], [[2g4n|2g4n]], [[2g4o|2g4o]], [[2g4p|2g4p]], [[2g4q|2g4q]], [[2g4r|2g4r]], [[2g4s|2g4s]], [[2g4t|2g4t]], [[2g4u|2g4u]], [[2g4v|2g4v]], [[2g4w|2g4w]], [[2g4x|2g4x]], [[2g4y|2g4y]], [[2g4z|2g4z]], [[2g51|2g51]], [[2g52|2g52]], [[2g55|2g55]]</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydroxynitrilase Hydroxynitrilase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.2.37 4.1.2.37] </span></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='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=2g4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g4l OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2g4l RCSB], [http://www.ebi.ac.uk/pdbsum/2g4l PDBsum]</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=2g4l FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2g4l OCA], [http://pdbe.org/2g4l PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2g4l RCSB], [http://www.ebi.ac.uk/pdbsum/2g4l PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 29: / Line 29: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 2g4l" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
@@ Line 34: / Line 35: @@
 </StructureSection>
 [[Category: Hevea brasiliensis]]
-[[Category: Hydroxynitrilase]]
+[[Category: Lyase]]
 [[Category: Mueller-Dieckmann, C]]
 [[Category: Weiss, M S]]
 [[Category: Anomalous substructure of hydroxynitrile lyase]]
-[[Category: Lyase]]

2g4l

From Proteopedia

Revision as of 02:28, 11 September 2015

Anomalous substructure of hydroxynitrile lyase

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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