4eah: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
New page: '''Unreleased structure''' The entry 4eah is ON HOLD Authors: Thompson, M.E., Heimsath, E.G., Gauvin, T.J, Higgs, H.N., Kull, F.J. Description: Crystal structure of the formin homology...
 
No edit summary
 
(11 intermediate revisions by the same user not shown)
Line 1: Line 1:
'''Unreleased structure'''


The entry 4eah is ON HOLD
==Crystal structure of the formin homology 2 domain of FMNL3 bound to actin==
<StructureSection load='4eah' size='340' side='right'caption='[[4eah]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[4eah]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EAH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene></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=4eah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4eah OCA], [https://pdbe.org/4eah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4eah RCSB], [https://www.ebi.ac.uk/pdbsum/4eah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4eah ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACTS_RABIT ACTS_RABIT] Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.


Authors: Thompson, M.E., Heimsath, E.G., Gauvin, T.J, Higgs, H.N., Kull, F.J.
==See Also==
 
*[[Actin 3D structures|Actin 3D structures]]
Description: Crystal structure of the formin homology 2 domain of FMNL3 bound to actin.
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Oryctolagus cuniculus]]
[[Category: Gauvin TJ]]
[[Category: Heimsath EG]]
[[Category: Higgs HN]]
[[Category: Kull FJ]]
[[Category: Thompson ME]]

Latest revision as of 14:02, 1 March 2024

Crystal structure of the formin homology 2 domain of FMNL3 bound to actinCrystal structure of the formin homology 2 domain of FMNL3 bound to actin

Structural highlights

4eah is a 8 chain structure with sequence from Mus musculus and Oryctolagus cuniculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3.4Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ACTS_RABIT Actins are highly conserved proteins that are involved in various types of cell motility and are ubiquitously expressed in all eukaryotic cells.

See Also

4eah, resolution 3.40Å

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