2emd: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
Line 2: Line 2:
<StructureSection load='2emd' size='340' side='right' caption='[[2emd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
<StructureSection load='2emd' size='340' side='right' caption='[[2emd]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2emd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aequorea_victoria Aequorea victoria]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EMD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EMD FirstGlance]. <br>
<table><tr><td colspan='2'>[[2emd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aeqvi Aeqvi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EMD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EMD FirstGlance]. <br>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSH:[2-(2-HYDROXY-1-METHYL-ETHYL)-4-(1H-IMIDAZOL-4-YLMETHYL)-5-OXO-IMIDAZOLIDIN-1-YL]-ACETIC+ACID'>CSH</scene></td></tr>
</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSH:[2-(2-HYDROXY-1-METHYL-ETHYL)-4-(1H-IMIDAZOL-4-YLMETHYL)-5-OXO-IMIDAZOLIDIN-1-YL]-ACETIC+ACID'>CSH</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1emc|1emc]], [[1eme|1eme]], [[1emf|1emf]], [[1emk|1emk]], [[1eml|1eml]], [[1emm|1emm]], [[2emn|2emn]], [[2emo|2emo]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1emc|1emc]], [[1eme|1eme]], [[1emf|1emf]], [[1emk|1emk]], [[1eml|1eml]], [[1emm|1emm]], [[2emn|2emn]], [[2emo|2emo]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GFP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6100 Aequorea victoria])</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">GFP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=6100 AEQVI])</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=2emd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2emd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2emd RCSB], [http://www.ebi.ac.uk/pdbsum/2emd 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=2emd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2emd OCA], [http://pdbe.org/2emd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2emd RCSB], [http://www.ebi.ac.uk/pdbsum/2emd PDBsum]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
Line 25: Line 25:
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Aequorea victoria]]
[[Category: Aeqvi]]
[[Category: Palm, G]]
[[Category: Palm, G]]
[[Category: Wlodawer, A]]
[[Category: Wlodawer, A]]

Revision as of 22:04, 10 September 2015

GREEN FLUORESCENT PROTEIN FROM AEQUOREA VICTORIA, MUTANTGREEN FLUORESCENT PROTEIN FROM AEQUOREA VICTORIA, MUTANT

Structural highlights

2emd is a 1 chain structure with sequence from Aeqvi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Gene:GFP (AEQVI)
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[GFP_AEQVI] Energy-transfer acceptor. Its role is to transduce the blue chemiluminescence of the protein aequorin into green fluorescent light by energy transfer. Fluoresces in vivo upon receiving energy from the Ca(2+)-activated photoprotein aequorin.

Evolutionary Conservation

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

See Also

2emd, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA