1k38: 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>
   </jmolCheckbox>
   </jmolCheckbox>
</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=1k38 ConSurf].
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Revision as of 21:48, 9 February 2016

CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-2CRYSTAL STRUCTURE OF THE CLASS D BETA-LACTAMASE OXA-2

Structural highlights

1k38 is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
NonStd Res:
Activity:Beta-lactamase, with EC number 3.5.2.6
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[BLO2_SALTM] This is an oxacillin-hydrolyzing beta-lactamase.

Evolutionary Conservation

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

See Also

1k38, resolution 1.50Å

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

OCA