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3qu1

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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=3qu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qu1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qu1 RCSB], [http://www.ebi.ac.uk/pdbsum/3qu1 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=3qu1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qu1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qu1 RCSB], [http://www.ebi.ac.uk/pdbsum/3qu1 PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/DEF2_VIBCH DEF2_VIBCH]] Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity).
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</StructureSection>
</StructureSection>

Revision as of 14:00, 25 December 2014

Peptide deformylase from Vibrio cholerae

3qu1, resolution 1.80Å

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