2pan: Difference between revisions

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'''Crystal structure of E. coli glyoxylate carboligase'''<br />

2PAN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=FAD:'>FAD</scene>, <scene name='pdbligand=TDP:'>TDP</scene>, <scene name='pdbligand=DTT:'>DTT</scene> and <scene name='pdbligand=1PE:'>1PE</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Tartronate-semialdehyde_synthase Tartronate-semialdehyde synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.47 4.1.1.47] Known structural/functional Sites: <scene name='pdbsite=AC1:Mg+Binding+Site+For+Residue+A+851'>AC1</scene>, <scene name='pdbsite=AC2:Mg+Binding+Site+For+Residue+B+851'>AC2</scene>, <scene name='pdbsite=AC3:Mg+Binding+Site+For+Residue+C+851'>AC3</scene>, <scene name='pdbsite=AC4:Mg+Binding+Site+For+Residue+D+851'>AC4</scene>, <scene name='pdbsite=AC5:Mg+Binding+Site+For+Residue+E+851'>AC5</scene>, <scene name='pdbsite=AC6:Mg+Binding+Site+For+Residue+F+851'>AC6</scene>, <scene name='pdbsite=AC7:Mg+Binding+Site+For+Residue+A+1501'>AC7</scene>, <scene name='pdbsite=AC8:Mg+Binding+Site+For+Residue+B+1501'>AC8</scene>, <scene name='pdbsite=AC9:Mg+Binding+Site+For+Residue+E+1501'>AC9</scene>, <scene name='pdbsite=BC1:Mg+Binding+Site+For+Residue+F+1501'>BC1</scene>, <scene name='pdbsite=BC2:Fad+Binding+Site+For+Residue+A+701'>BC2</scene>, <scene name='pdbsite=BC3:Tdp+Binding+Site+For+Residue+A+801'>BC3</scene>, <scene name='pdbsite=BC4:Dtt+Binding+Site+For+Residue+A+901'>BC4</scene>, <scene name='pdbsite=BC5:Fad+Binding+Site+For+Residue+B+701'>BC5</scene>, <scene name='pdbsite=BC6:Tdp+Binding+Site+For+Residue+B+801'>BC6</scene>, <scene name='pdbsite=BC7:Dtt+Binding+Site+For+Residue+B+901'>BC7</scene>, <scene name='pdbsite=BC8:Fad+Binding+Site+For+Residue+C+701'>BC8</scene>, <scene name='pdbsite=BC9:Tdp+Binding+Site+For+Residue+C+801'>BC9</scene>, <scene name='pdbsite=CC1:Dtt+Binding+Site+For+Residue+C+901'>CC1</scene>, <scene name='pdbsite=CC2:Fad+Binding+Site+For+Residue+D+701'>CC2</scene>, <scene name='pdbsite=CC3:Tdp+Binding+Site+For+Residue+D+801'>CC3</scene>, <scene name='pdbsite=CC4:Dtt+Binding+Site+For+Residue+D+901'>CC4</scene>, <scene name='pdbsite=CC5:Fad+Binding+Site+For+Residue+E+701'>CC5</scene>, <scene name='pdbsite=CC6:Tdp+Binding+Site+For+Residue+E+801'>CC6</scene>, <scene name='pdbsite=CC7:Dtt+Binding+Site+For+Residue+E+901'>CC7</scene>, <scene name='pdbsite=CC8:Fad+Binding+Site+For+Residue+F+701'>CC8</scene>, <scene name='pdbsite=CC9:Tdp+Binding+Site+For+Residue+F+801'>CC9</scene>, <scene name='pdbsite=DC1:Dtt+Binding+Site+For+Residue+F+901'>DC1</scene> and <scene name='pdbsite=DC2:1pe+Binding+Site+For+Residue+A+951'>DC2</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PAN OCA].  

Glyoxylate carboligase lacks the canonical active site glutamate of thiamine-dependent enzymes., Kaplun A, Binshtein E, Vyazmensky M, Steinmetz A, Barak Z, Chipman DM, Tittmann K, Shaanan B, Nat Chem Biol. 2008 Feb;4(2):113-8. Epub 2008 Jan 6. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=18176558 18176558]

[[Category: thimain-dependent enzymes]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:27:49 2008''