1up5

From Proteopedia

(Difference between revisions)

Revision as of 10:28, 17 February 2021

Chicken Calmodulin

Structural highlights

1up5 is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Related:	1a29, 1ahr, 1aji, 1ak8, 1cdl, 1cdm, 1cfc, 1cfd, 1cff, 1ckk, 1cll, 1cm1, 1cm4, 1cmf, 1cmg, 1ctr, 1deg, 1dmo, 1f70, 1f71, 1fw4, 1iq5, 1iwq, 1j7o, 1j7p, 1k90, 1k93, 1l7z, 1lin, 1lvc, 1mux, 1nkf, 1nwd, 1qiv, 1qiw, 2cln, 3cln
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CALM_CHICK] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.

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

Two new crystal forms of calmodulin from Gallus gallus are reported. Crystals in space group P1 (cell dimensions a = 59.7, b = 53.1, c = 24.6 A, alpha = 93.2, beta = 96.7, gamma = 89.2 and Z = 2), grow as long thin needles. Water content on density considerations is approximately 50%. They diffract to approximately 2.0 A but give wide multiply peaked spot profiles. Crystals in space group P2(1)2(1)2(1) (cell dimensions a = 32.2, b = 56.0, c = 67.3 A and Z = 4), grow as clusters of thin tablets and contain approximately 30% water by volume. These small crystals ( approximately 0.4 x 0.15 x 0.1 mm) diffracted well to approximately 1.4 A and some appreciable intensities were observed at resolutions better than 1.2 A.

Crystallization and preliminary X-ray analysis of two new crystal forms of calmodulin.,Rupp B, Marshak DR, Parkin S Acta Crystallogr D Biol Crystallogr. 1996 Mar 1;52(Pt 2):411-3. PMID:15299715^[1]

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

References

↑ Rupp B, Marshak DR, Parkin S. Crystallization and preliminary X-ray analysis of two new crystal forms of calmodulin. Acta Crystallogr D Biol Crystallogr. 1996 Mar 1;52(Pt 2):411-3. PMID:15299715 doi:10.1107/S0907444995011826

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1up5"

@@ Line 3: / Line 3: @@
 <StructureSection load='1up5' size='340' side='right'caption='[[1up5]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1up5]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UP5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UP5 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1up5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UP5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UP5 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=M3L:N-TRIMETHYLLYSINE'>M3L</scene></td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1a29|1a29]], [[1ahr|1ahr]], [[1aji|1aji]], [[1ak8|1ak8]], [[1cdl|1cdl]], [[1cdm|1cdm]], [[1cfc|1cfc]], [[1cfd|1cfd]], [[1cff|1cff]], [[1ckk|1ckk]], [[1cll|1cll]], [[1cm1|1cm1]], [[1cm4|1cm4]], [[1cmf|1cmf]], [[1cmg|1cmg]], [[1ctr|1ctr]], [[1deg|1deg]], [[1dmo|1dmo]], [[1f70|1f70]], [[1f71|1f71]], [[1fw4|1fw4]], [[1iq5|1iq5]], [[1iwq|1iwq]], [[1j7o|1j7o]], [[1j7p|1j7p]], [[1k90|1k90]], [[1k93|1k93]], [[1l7z|1l7z]], [[1lin|1lin]], [[1lvc|1lvc]], [[1mux|1mux]], [[1nkf|1nkf]], [[1nwd|1nwd]], [[1qiv|1qiv]], [[1qiw|1qiw]], [[2cln|2cln]], [[3cln|3cln]]</td></tr>
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1a29|1a29]], [[1ahr|1ahr]], [[1aji|1aji]], [[1ak8|1ak8]], [[1cdl|1cdl]], [[1cdm|1cdm]], [[1cfc|1cfc]], [[1cfd|1cfd]], [[1cff|1cff]], [[1ckk|1ckk]], [[1cll|1cll]], [[1cm1|1cm1]], [[1cm4|1cm4]], [[1cmf|1cmf]], [[1cmg|1cmg]], [[1ctr|1ctr]], [[1deg|1deg]], [[1dmo|1dmo]], [[1f70|1f70]], [[1f71|1f71]], [[1fw4|1fw4]], [[1iq5|1iq5]], [[1iwq|1iwq]], [[1j7o|1j7o]], [[1j7p|1j7p]], [[1k90|1k90]], [[1k93|1k93]], [[1l7z|1l7z]], [[1lin|1lin]], [[1lvc|1lvc]], [[1mux|1mux]], [[1nkf|1nkf]], [[1nwd|1nwd]], [[1qiv|1qiv]], [[1qiw|1qiw]], [[2cln|2cln]], [[3cln|3cln]]</div></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=1up5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1up5 OCA], [http://pdbe.org/1up5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1up5 RCSB], [http://www.ebi.ac.uk/pdbsum/1up5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1up5 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=1up5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1up5 OCA], [https://pdbe.org/1up5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1up5 RCSB], [https://www.ebi.ac.uk/pdbsum/1up5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1up5 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CALM_CHICK CALM_CHICK]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
+[[https://www.uniprot.org/uniprot/CALM_CHICK CALM_CHICK]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1up5

From Proteopedia

Revision as of 10:28, 17 February 2021

Chicken Calmodulin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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