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1xrl

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<StructureSection load='1xrl' size='340' side='right'caption='[[1xrl]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
<StructureSection load='1xrl' size='340' side='right'caption='[[1xrl]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1xrl]] 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=1XRL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1XRL FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1xrl]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoplasma_acidophilum Thermoplasma acidophilum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XRL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1XRL FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PHK:(2R,3S)-3-AMINO-1-CHLORO-4-PHENYL-BUTAN-2-OL'>PHK</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]] 1.82&#8491;</td></tr>
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<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]], [[1xrm|1xrm]], [[1xrn|1xrn]], [[1xro|1xro]], [[1xrp|1xrp]], [[1xrq|1xrq]], [[1xrr|1xrr]]</div></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=PHK:(2R,3S)-3-AMINO-1-CHLORO-4-PHENYL-BUTAN-2-OL'>PHK</scene></td></tr>
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<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>
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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=1xrl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrl OCA], [https://pdbe.org/1xrl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xrl RCSB], [https://www.ebi.ac.uk/pdbsum/1xrl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xrl ProSAT]</span></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/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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1xrl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xrl OCA], [http://pdbe.org/1xrl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1xrl RCSB], [http://www.ebi.ac.uk/pdbsum/1xrl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1xrl ProSAT]</span></td></tr>
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</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/PIP_THEAC PIP_THEAC]] Cleaves H-Pro-AMC as well as a wide spectrum of amino acid substrates and several peptide substrates without a proline at the N-terminus. Proteases F1, F2 and F3 degrade oligopeptides produced by Tricorn (themselves probably produced by the proteasome) yielding free amino acids.
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[https://www.uniprot.org/uniprot/PIP_THEAC PIP_THEAC] Cleaves H-Pro-AMC as well as a wide spectrum of amino acid substrates and several peptide substrates without a proline at the N-terminus. Proteases F1, F2 and F3 degrade oligopeptides produced by Tricorn (themselves probably produced by the proteasome) yielding free amino acids.
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Prolyl aminopeptidase]]
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[[Category: Thermoplasma acidophilum]]
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[[Category: Brandstetter, H]]
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[[Category: Brandstetter H]]
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[[Category: Goehring, W]]
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[[Category: Goehring W]]
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[[Category: Goettig, P]]
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[[Category: Goettig P]]
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[[Category: Groll, M]]
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[[Category: Groll M]]
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[[Category: Huber, R]]
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[[Category: Huber R]]
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[[Category: Kim, J S]]
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[[Category: Kim J-S]]
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[[Category: Konarev, P V]]
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[[Category: Konarev PV]]
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[[Category: Svergun, D I]]
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[[Category: Svergun DI]]
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[[Category: Alpha-beta hydrolase]]
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[[Category: Caged active site]]
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[[Category: Chloromethyl ketone inhibitor]]
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[[Category: Hydrogen bonded network]]
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[[Category: Hydrolase]]
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[[Category: Substrate recognition]]
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Current revision

Crystal structure of active site F1-mutant Y205F complex with inhibitor PCK

PDB ID 1xrl

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