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1xro
From Proteopedia
(Difference between revisions)
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==Crystal structure of active site F1-mutant E213Q soaked with peptide Phe-Leu== | ==Crystal structure of active site F1-mutant E213Q soaked with peptide Phe-Leu== | ||
| - | <StructureSection load='1xro' size='340' side='right' caption='[[1xro]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='1xro' size='340' side='right'caption='[[1xro]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1xro]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRO OCA]. For a <b>guided tour on the structure components</b> use [http:// | + | <table><tr><td colspan='2'>[[1xro]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"thermoplasma_acidophila"_(sic)_darland_et_al._1970 "thermoplasma acidophila" (sic) darland et al. 1970]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRO OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XRO FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LEU:LEUCINE'>LEU</scene></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1mtz|1mtz]], [[1mu0|1mu0]], [[1mt3|1mt3]], [[1xqv|1xqv]], [[1xqw|1xqw]], [[1xqx|1xqx]], [[1xqy|1xqy]], [[1xrl|1xrl]], [[1xrm|1xrm]], [[1xrn|1xrn]], [[1xrp|1xrp]], [[1xrq|1xrq]], [[1xrr|1xrr]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1mtz|1mtz]], [[1mu0|1mu0]], [[1mt3|1mt3]], [[1xqv|1xqv]], [[1xqw|1xqw]], [[1xqx|1xqx]], [[1xqy|1xqy]], [[1xrl|1xrl]], [[1xrm|1xrm]], [[1xrn|1xrn]], [[1xrp|1xrp]], [[1xrq|1xrq]], [[1xrr|1xrr]]</div></td></tr> |
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">TA0830 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2303 "Thermoplasma acidophila" (sic) Darland et al. 1970])</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Prolyl_aminopeptidase Prolyl aminopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.11.5 3.4.11.5] </span></td></tr> | ||
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http:// | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1xro FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xro OCA], [http://pdbe.org/1xro PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xro RCSB], [http://www.ebi.ac.uk/pdbsum/1xro PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xro ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
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==See Also== | ==See Also== | ||
| - | *[[Aminopeptidase|Aminopeptidase]] | + | *[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]] |
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
[[Category: Prolyl aminopeptidase]] | [[Category: Prolyl aminopeptidase]] | ||
[[Category: Brandstetter, H]] | [[Category: Brandstetter, H]] | ||
Revision as of 10:17, 6 January 2021
Crystal structure of active site F1-mutant E213Q soaked with peptide Phe-Leu
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