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4f8z
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Carboxypeptidase T with Boc-Leu== | |
| + | <StructureSection load='4f8z' size='340' side='right'caption='[[4f8z]], [[Resolution|resolution]] 1.38Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[4f8z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermoactinomyces_vulgaris Thermoactinomyces vulgaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4F8Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4F8Z FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BL2:N-(TERT-BUTOXYCARBONYL)-L-LEUCINE'>BL2</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4f8z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4f8z OCA], [https://pdbe.org/4f8z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4f8z RCSB], [https://www.ebi.ac.uk/pdbsum/4f8z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4f8z ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CBPT_THEVU CBPT_THEVU] Able to split off hydrophobic and basic amino acids with comparable efficiency. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The 3D structure of recombinant bacterial carboxypeptidase T (CPT) in complex with N-BOC-L-leucine was determined at 1.38 A resolution. Crystals for the X-ray study were grown in microgravity using the counter-diffusion technique. N-BOC-L-leucine and SO4(2-) ion bound in the enzyme active site were localized in the electron density map. Location of the leucine side chain in CPT-N-BOC-L-leucine complex allowed identification of the S1 subsite of the enzyme, and its structure was determined. Superposition of the structures of CPT-N-BOC-L-leucine complex and complexes of pancreatic carboxypeptidases A and B with substrate and inhibitors was carried out, and similarity of the S1 subsites in these three carboxypeptidases was revealed. It was found that SO4(2-) ion occupies the same position in the S1' subsite as the C-terminal carboxy group of the substrate. | ||
| - | + | Three-dimensional structure of carboxypeptidase T from Thermoactinomyces vulgaris in complex with N-BOC-L-leucine.,Timofeev VI, Kuznetsov SA, Akparov VKh, Chestukhina GG, Kuranova IP Biochemistry (Mosc). 2013 Mar;78(3):252-9. doi: 10.1134/S0006297913030061. PMID:23586718<ref>PMID:23586718</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| + | </div> | ||
| + | <div class="pdbe-citations 4f8z" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Carboxypeptidase 3D structures|Carboxypeptidase 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Thermoactinomyces vulgaris]] | ||
| + | [[Category: Akparov VK]] | ||
| + | [[Category: Kuranova IP]] | ||
| + | [[Category: Kuznetsov SA]] | ||
| + | [[Category: Timofeev VI]] | ||
Current revision
Carboxypeptidase T with Boc-Leu
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