5jf8

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==Crystal structure of type 2 PDF from Streptococcus agalactiae in complex with inhibitor RAS358 (21)==
==Crystal structure of type 2 PDF from Streptococcus agalactiae in complex with inhibitor RAS358 (21)==
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<StructureSection load='5jf8' size='340' side='right' caption='[[5jf8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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<StructureSection load='5jf8' size='340' side='right'caption='[[5jf8]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[5jf8]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JF8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JF8 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[5jf8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Streptococcus_agalactiae Streptococcus agalactiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JF8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JF8 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=PN3:TERT-BUTYL+{(2S)-1-[FORMYL(HYDROXY)AMINO]-3-PHENYLPROPAN-2-YL}CARBAMATE'>PN3</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=IMD:IMIDAZOLE'>IMD</scene>, <scene name='pdbligand=OCS:CYSTEINESULFONIC+ACID'>OCS</scene>, <scene name='pdbligand=PN3:TERT-BUTYL+{(2S)-1-[FORMYL(HYDROXY)AMINO]-3-PHENYLPROPAN-2-YL}CARBAMATE'>PN3</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5jf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jf8 OCA], [https://pdbe.org/5jf8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jf8 RCSB], [https://www.ebi.ac.uk/pdbsum/5jf8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jf8 ProSAT]</span></td></tr>
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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=5jf8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jf8 OCA], [http://pdbe.org/5jf8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jf8 RCSB], [http://www.ebi.ac.uk/pdbsum/5jf8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jf8 ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/DEF_STRA3 DEF_STRA3]] 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.
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[https://www.uniprot.org/uniprot/DEF_STRA3 DEF_STRA3] 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.
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Peptide deformylase]]
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[[Category: Large Structures]]
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[[Category: Fieulaine, S]]
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[[Category: Giglione, C]]
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[[Category: Meinnel, T]]
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[[Category: Hydrolase]]
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[[Category: Inhibitor]]
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[[Category: N-terminal methionine excision]]
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[[Category: Nme]]
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[[Category: Pdf]]
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[[Category: Ras358]]
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[[Category: Streptococcus agalactiae]]
[[Category: Streptococcus agalactiae]]
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[[Category: Type 2]]
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[[Category: Fieulaine S]]
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[[Category: Giglione C]]
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[[Category: Meinnel T]]

Current revision

Crystal structure of type 2 PDF from Streptococcus agalactiae in complex with inhibitor RAS358 (21)

PDB ID 5jf8

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