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3mr1
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=3mr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mr1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mr1 RCSB], [http://www.ebi.ac.uk/pdbsum/3mr1 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=3mr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mr1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3mr1 RCSB], [http://www.ebi.ac.uk/pdbsum/3mr1 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[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 17:03, 25 December 2014
Crystal structure of methionine aminopeptidase from Rickettsia prowazekii
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