2j3d: Difference between revisions

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     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2j3d ConSurf].
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==See Also==
==See Also==
*[[Acetylcholinesterase|Acetylcholinesterase]]
*[[3D structures of acetylcholinesterase|3D structures of acetylcholinesterase]]
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</StructureSection>
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Revision as of 05:19, 10 February 2016

NATIVE MONOCLINIC FORM OF TORPEDO ACETYLCHOLINESTERASENATIVE MONOCLINIC FORM OF TORPEDO ACETYLCHOLINESTERASE

Structural highlights

2j3d is a 1 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Activity:Acetylcholinesterase, with EC number 3.1.1.7
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[ACES_TORCA] Terminates signal transduction at the neuromuscular junction by rapid hydrolysis of the acetylcholine released into the synaptic cleft. May be involved in cell-cell interactions.

Evolutionary Conservation

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

See Also

2j3d, resolution 2.60Å

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OCA