2ex4
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2ex4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EX4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EX4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[2ex4]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EX4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2EX4 FirstGlance]. <br> | ||
- | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SAH:S-ADENOSYL-L-HOMOCYSTEINE'>SAH</scene></td></tr> |
- | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ex4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ex4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ex4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ex4 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=2ex4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ex4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2ex4 RCSB], [http://www.ebi.ac.uk/pdbsum/2ex4 PDBsum]</span></td></tr> |
- | <table> | + | </table> |
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/CI032_HUMAN CI032_HUMAN]] Distributive alpha-N-methyltransferase that methylates the N-terminus of target proteins containing the N-terminal motif [Ala/Pro/Ser]-Pro-Lys when the initiator Met is cleaved. Specifically catalyzes mono-, di- or tri-methylation of exposed alpha-amino group of Ala or Ser residue in the [Ala/Ser]-Pro-Lys motif and mono- or di-methylation of Pro in the Pro-Pro-Lys motif. Some of the substrates may be primed by METTL11B-mediated monomethylation. Responsible for the N-terminal methylation of KLHL31, MYL2, MYL3, RB1, RCC1, RPL23A and SET. Required during mitosis for normal bipolar spindle formation and chromosome segregation via its action on RCC1.<ref>PMID:20481588</ref> <ref>PMID:20668449</ref> <ref>PMID:24090352</ref> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
- | [[Category: Arrowsmith, C H | + | [[Category: Arrowsmith, C H]] |
- | [[Category: Bochkarev, A | + | [[Category: Bochkarev, A]] |
- | [[Category: Edwards, A M | + | [[Category: Edwards, A M]] |
- | [[Category: Loppnau, P | + | [[Category: Loppnau, P]] |
- | [[Category: Min, J R | + | [[Category: Min, J R]] |
- | [[Category: Plotnikov, A N | + | [[Category: Plotnikov, A N]] |
- | [[Category: | + | [[Category: Structural genomic]] |
- | [[Category: Sundstrom, M | + | [[Category: Sundstrom, M]] |
- | [[Category: Wu, H | + | [[Category: Wu, H]] |
- | [[Category: Zeng, H | + | [[Category: Zeng, H]] |
[[Category: Methyltransferase]] | [[Category: Methyltransferase]] | ||
[[Category: Sgc]] | [[Category: Sgc]] | ||
- | [[Category: Structural genomic]] | ||
- | [[Category: Structural genomics consortium]] | ||
[[Category: Transferase]] | [[Category: Transferase]] |
Revision as of 20:28, 25 December 2014
Crystal Structure of Human methyltransferase AD-003 in complex with S-adenosyl-L-homocysteine
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