3mx6

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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=3mx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mx6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mx6 RCSB], [http://www.ebi.ac.uk/pdbsum/3mx6 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=3mx6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mx6 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mx6 RCSB], [http://www.ebi.ac.uk/pdbsum/3mx6 PDBsum]</span></td></tr>
</table>
</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/AMPM_RICPR AMPM_RICPR]] Removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). Requires deformylation of the N(alpha)-formylated initiator methionine before it can be hydrolyzed.[HAMAP-Rule:MF_01974]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 22:09, 24 December 2014

Crystal structure of methionine aminopeptidase from Rickettsia prowazekii bound to methionine

3mx6, resolution 1.70Å

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