3oca
From Proteopedia
(Difference between revisions)
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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=3oca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oca OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oca RCSB], [http://www.ebi.ac.uk/pdbsum/3oca 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=3oca FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3oca OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3oca RCSB], [http://www.ebi.ac.uk/pdbsum/3oca PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/Q2GI30_EHRCR Q2GI30_EHRCR]] 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).[HAMAP-Rule:MF_00163] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Revision as of 01:29, 25 December 2014
Crystal structure of peptide deformylase from Ehrlichia chaffeensis
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