3l87
From Proteopedia
(Difference between revisions)
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<StructureSection load='3l87' size='340' side='right' caption='[[3l87]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='3l87' size='340' side='right' caption='[[3l87]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[3l87]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L87 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L87 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3l87]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Strmu Strmu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3L87 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3L87 FirstGlance]. <br> |
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FE:FE+(III)+ION'>FE</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=CSD:3-SULFINOALANINE'>CSD</scene></td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">smu.143c ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210007 STRMU])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide_deformylase Peptide deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.88 3.5.1.88] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptide_deformylase Peptide deformylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.1.88 3.5.1.88] </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=3l87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l87 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l87 RCSB], [http://www.ebi.ac.uk/pdbsum/3l87 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=3l87 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3l87 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3l87 RCSB], [http://www.ebi.ac.uk/pdbsum/3l87 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/DEF_STRMU DEF_STRMU]] 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). | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Peptide deformylase]] | [[Category: Peptide deformylase]] | ||
| + | [[Category: Strmu]] | ||
[[Category: Cao, Q]] | [[Category: Cao, Q]] | ||
[[Category: Liu, X]] | [[Category: Liu, X]] | ||
Revision as of 23:03, 24 December 2014
The Crystal Structure of smu.143c from Streptococcus mutans UA159
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Categories: Peptide deformylase | Strmu | Cao, Q | Liu, X | Su, X D | Def | Hydrolase | Iron | Metal-binding | Protein biosynthesis
