5cx0: Difference between revisions

Line 1:

~~'''Unreleased structure'''~~

~~The entry~~ 5cx0 is ~~ON HOLD until Paper Publication~~

==Structure of Xoo1075, a peptide deformylase from Xanthomonas oryzae pv. oryzae, in complex with fragment 322==

~~Authors~~: ~~Ngo~~, H.P.T., ~~Kang~~, L.W.

== Structural highlights ==

<table><tr><td colspan='2'>[[5cx0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CX0 OCA]. For a guided tour on the structure components use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CX0 FirstGlance].

~~Description~~: ~~Structure~~ of ~~Xoo1075,~~ a ~~peptide deformylase from Xanthomonas oryzae pv~~. ~~oryzae, in complex with fragment 322~~

</td></tr><tr id='ligand'><td class="sblockLbl">[[Ligand|Ligands:]]</td><td class="sblockDat"><scene name='pdbligand=56L:5-(PROPAN-2-YL)-2-THIOXODIHYDROPYRIMIDINE-4,6(1H,5H)-DIONE'>56L</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>

[[Category: ~~Unreleased Structures~~]]

[[Category: Kang, L.W]]

<tr id='activity'><td class="sblockLbl">Activity:</td><td class="sblockDat">[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] </td></tr>

[[Category: Ngo, H.P.T]]

<tr id='resources'><td class="sblockLbl">Resources:</td><td class="sblockDat">[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5cx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cx0 OCA], [http://pdbe.org/5cx0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cx0 RCSB], [http://www.ebi.ac.uk/pdbsum/5cx0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cx0 ProSAT]</td></tr>

</table>

== Function ==

[[http://www.uniprot.org/uniprot/Q5H3Z2_XANOR Q5H3Z2_XANOR]] 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.[HAMAP-Rule:MF_00163]

__TOC__

</StructureSection>

[[Category: Peptide deformylase]]

[[Category: Kang, L W]]

[[Category: Ngo, H P.T]]

[[Category: Fragment]]

[[Category: Hydrolase]]

[[Category: Metallopeptidase]]

[[Category: Peptide deformyase]]

[[Category: Xanthomona]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 5cx0 is ON HOLD  until Paper Publication
+==Structure of Xoo1075, a peptide deformylase from Xanthomonas oryzae pv. oryzae, in complex with fragment 322==
+<StructureSection load='5cx0' size='340' side='right' caption='[[5cx0]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-Authors: Ngo, H.P.T., Kang, L.W.
+== Structural highlights ==
+<table><tr><td colspan='2'>[[5cx0]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CX0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5CX0 FirstGlance]. <br>
-Description: Structure of Xoo1075, a peptide deformylase from Xanthomonas oryzae pv. oryzae, in complex with fragment 322
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=56L:5-(PROPAN-2-YL)-2-THIOXODIHYDROPYRIMIDINE-4,6(1H,5H)-DIONE'>56L</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene></td></tr>
-[[Category: Unreleased Structures]]
+<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5cp0|5cp0]], [[5cpd|5cpd]], [[5cvk|5cvk]], [[5cvp|5cvp]], [[5cvq|5cvq]], [[5cwx|5cwx]], [[5cwy|5cwy]], [[5cxj|5cxj]], [[5cy7|5cy7]], [[5cy8|5cy8]]</td></tr>
-[[Category: Kang, L.W]]
+<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>
-[[Category: Ngo, H.P.T]]
+<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=5cx0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5cx0 OCA], [http://pdbe.org/5cx0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5cx0 RCSB], [http://www.ebi.ac.uk/pdbsum/5cx0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5cx0 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[[http://www.uniprot.org/uniprot/Q5H3Z2_XANOR Q5H3Z2_XANOR]] 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.[HAMAP-Rule:MF_00163]
+__TOC__
+</StructureSection>
+[[Category: Peptide deformylase]]
+[[Category: Kang, L W]]
+[[Category: Ngo, H P.T]]
+[[Category: Fragment]]
+[[Category: Hydrolase]]
+[[Category: Metallopeptidase]]
+[[Category: Peptide deformyase]]
+[[Category: Xanthomona]]