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1cq7
From Proteopedia
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<StructureSection load='1cq7' size='340' side='right'caption='[[1cq7]], [[Resolution|resolution]] 2.40Å' scene=''> | <StructureSection load='1cq7' size='340' side='right'caption='[[1cq7]], [[Resolution|resolution]] 2.40Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1cq7]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQ7 OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[1cq7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQ7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CQ7 FirstGlance]. <br> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.4Å</td></tr> |
| - | <tr id=' | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PY5:2-[O-PHOSPHONOPYRIDOXYL]-AMINO-PENTANOIC+ACID'>PY5</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=1cq7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cq7 OCA], [https://pdbe.org/1cq7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cq7 RCSB], [https://www.ebi.ac.uk/pdbsum/1cq7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cq7 ProSAT]</span></td></tr> | |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | |
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/AAT_ECOLI AAT_ECOLI] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cq7 ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cq7 ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | Domain movement is sometimes essential for substrate recognition by an enzyme. X-ray crystallography of aminotransferase with a series of aliphatic substrates showed that the domain movement of aspartate aminotransferase was changed dramatically from an open to a closed form by the addition of only one CH(2) to the side chain of the C4 substrate CH(3)(CH(2))C((alpha))H(NH(3)(+))COO(-). These crystallographic results and reaction kinetics (Kawaguchi, S., Nobe, Y., Yasuoka, J., Wakamiya, T., Kusumoto, S., and Kuramitsu, S. (1997) J. Biochem. (Tokyo) 122, 55-63; Kawaguchi, S. and Kuramitsu, S. (1998) J. Biol. Chem. 273, 18353-18364) enabled us to estimate the free energy required for the domain movement. | ||
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| - | Free energy requirement for domain movement of an enzyme.,Ishijima J, Nakai T, Kawaguchi S, Hirotsu K, Kuramitsu S J Biol Chem. 2000 Jun 23;275(25):18939-45. PMID:10858450<ref>PMID:10858450</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1cq7" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]] | *[[Aspartate aminotransferase 3D structures|Aspartate aminotransferase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: | + | [[Category: Escherichia coli]] |
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: Hirotsu | + | [[Category: Hirotsu K]] |
| - | [[Category: Ishijima | + | [[Category: Ishijima J]] |
| - | [[Category: Kawaguchi | + | [[Category: Kawaguchi S]] |
| - | [[Category: Kuramitsu | + | [[Category: Kuramitsu S]] |
| - | [[Category: Nakai | + | [[Category: Nakai T]] |
| - | + | ||
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Current revision
ASPARTATE AMINOTRANSFERASE (E.C. 2.6.1.1) COMPLEXED WITH C5-PYRIDOXAL-5P-PHOSPHATE
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