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The | ==Human methionine aminopeptidase type 1b (F309M mutant) in complex with ovalicin== | ||
<StructureSection load='5ykp' size='340' side='right' caption='[[5ykp]], [[Resolution|resolution]] 1.68Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ykp]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YKP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5YKP FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CO:COBALT+(II)+ION'>CO</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=OVA:3,4-DIHYDROXY-2-METHOXY-4-METHYL-3-[2-METHYL-3-(3-METHYL-BUT-2-ENYL)+-OXIRANYL]-CYCLOHEXANONE'>OVA</scene></td></tr> | |||
[[Category: | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Methionyl_aminopeptidase Methionyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.18 3.4.11.18] </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=5ykp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ykp OCA], [http://pdbe.org/5ykp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5ykp RCSB], [http://www.ebi.ac.uk/pdbsum/5ykp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5ykp ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[[http://www.uniprot.org/uniprot/MAP11_HUMAN MAP11_HUMAN]] Cotranslationally 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). Required for normal progression through the cell cycle.[HAMAP-Rule:MF_03174]<ref>PMID:16274222</ref> <ref>PMID:17114291</ref> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Methionyl aminopeptidase]] | |||
[[Category: Addlagatta, A]] | |||
[[Category: Arya, T]] | |||
[[Category: Pillalamarri, V]] | |||
[[Category: Enterococcus feacali]] | |||
[[Category: Metal binding protein]] | |||
[[Category: Selective inhibition]] | |||
[[Category: Streptococcal pneumoniae]] |
Revision as of 10:50, 17 October 2018
Human methionine aminopeptidase type 1b (F309M mutant) in complex with ovalicinHuman methionine aminopeptidase type 1b (F309M mutant) in complex with ovalicin
Structural highlights
Function[MAP11_HUMAN] Cotranslationally 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). Required for normal progression through the cell cycle.[HAMAP-Rule:MF_03174][1] [2] References
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