3mxu

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<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=3mxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mxu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mxu RCSB], [http://www.ebi.ac.uk/pdbsum/3mxu 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=3mxu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mxu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mxu RCSB], [http://www.ebi.ac.uk/pdbsum/3mxu PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/GCSH_BARHE GCSH_BARHE]] The glycine cleavage system catalyzes the degradation of glycine. The H protein shuttles the methylamine group of glycine from the P protein to the T protein (By similarity).
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 10:15, 25 December 2014

Crystal structure of glycine cleavage system protein H from Bartonella henselae

3mxu, resolution 1.80Å

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