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4chi

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Current revision (17:46, 7 September 2022) (edit) (undo)
 
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<StructureSection load='4chi' size='340' side='right'caption='[[4chi]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
<StructureSection load='4chi' size='340' side='right'caption='[[4chi]], [[Resolution|resolution]] 1.27&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4chi]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfu Aspfu]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHI OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CHI FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4chi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus_Af293 Aspergillus fumigatus Af293]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CHI 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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
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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=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=4chi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4chi OCA], [http://pdbe.org/4chi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4chi RCSB], [http://www.ebi.ac.uk/pdbsum/4chi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4chi ProSAT]</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=4chi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4chi OCA], [https://pdbe.org/4chi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4chi RCSB], [https://www.ebi.ac.uk/pdbsum/4chi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4chi ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[[https://www.uniprot.org/uniprot/Q4WH08_ASPFU Q4WH08_ASPFU]]
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The importance of amine transaminases for producing optically pure chiral precursors for pharmaceuticals and chemicals has substantially increased in recent years. The X-ray crystal structure of the (R)-selective amine transaminase from the fungus Aspergillus fumigatus was solved by S-SAD phasing to 1.84 A resolution. The refined structure at 1.27 A resolution provides detailed knowledge about the molecular basis of substrate recognition and conversion to facilitate protein-engineering approaches. The protein forms a homodimer and belongs to fold class IV of the pyridoxal-5'-phosphate-dependent enzymes. Both subunits contribute residues to form two active sites. The structure of the holoenzyme shows the catalytically important cofactor pyridoxal-5'-phosphate bound as an internal aldimine with the catalytically responsible amino-acid residue Lys179, as well as in its free form. A long N-terminal helix is an important feature for the stability of this fungal (R)-selective amine transaminase, but is missing in branched-chain amino-acid aminotransferases and D-amino-acid aminotransferases.
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Crystallographic characterization of the (R)-selective amine transaminase from Aspergillus fumigatus.,Thomsen M, Skalden L, Palm GJ, Hohne M, Bornscheuer UT, Hinrichs W Acta Crystallogr D Biol Crystallogr. 2014 Apr 1;70(Pt 4):1086-93. doi:, 10.1107/S1399004714001084. Epub 2014 Mar 20. PMID:24699652<ref>PMID:24699652</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4chi" style="background-color:#fffaf0;"></div>
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==See Also==
==See Also==
*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
*[[Aminotransferase 3D structures|Aminotransferase 3D structures]]
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Aspfu]]
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[[Category: Aspergillus fumigatus Af293]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Hinrichs, W]]
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[[Category: Hinrichs W]]
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[[Category: Palm, G J]]
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[[Category: Palm GJ]]
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[[Category: Thomsen, M]]
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[[Category: Thomsen M]]
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[[Category: Transferase]]
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Current revision

(R)-selective amine transaminase from Aspergillus fumigatus at 1.27 A resolution

PDB ID 4chi

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