2c4m: 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=2c4m ConSurf].
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Revision as of 17:42, 9 February 2016

STARCH PHOSPHORYLASE: STRUCTURAL STUDIES EXPLAIN OXYANION-DEPENDENT KINETIC STABILITY AND REGULATORY CONTROL.STARCH PHOSPHORYLASE: STRUCTURAL STUDIES EXPLAIN OXYANION-DEPENDENT KINETIC STABILITY AND REGULATORY CONTROL.

Structural highlights

2c4m is a 4 chain structure with sequence from Atcc 15991. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, , ,
Activity:Phosphorylase, with EC number 2.4.1.1
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[Q8KQ56_9CORY] Phosphorylase is an important allosteric enzyme in carbohydrate metabolism. Enzymes from different sources differ in their regulatory mechanisms and in their natural substrates. However, all known phosphorylases share catalytic and structural properties.[RuleBase:RU000587]

Evolutionary Conservation

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

See Also

2c4m, resolution 1.90Å

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OCA