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1qf4
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1qf4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QF4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QF4 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1qf4]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QF4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1QF4 FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=RPD:(C8-R)-HYDANTOCIDIN+5-PHOSPHATE'>RPD</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene>, <scene name='pdbligand=RPD:(C8-R)-HYDANTOCIDIN+5-PHOSPHATE'>RPD</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylosuccinate_synthase Adenylosuccinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.4 6.3.4.4] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Adenylosuccinate_synthase Adenylosuccinate synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.3.4.4 6.3.4.4] </span></td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qf4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qf4 RCSB], [http://www.ebi.ac.uk/pdbsum/1qf4 PDBsum]</span></td></tr> | + | <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=1qf4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qf4 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1qf4 RCSB], [http://www.ebi.ac.uk/pdbsum/1qf4 PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/PURA_ECOLI PURA_ECOLI]] Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP (By similarity).[HAMAP-Rule:MF_00011] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Adenylosuccinate synthase]] | [[Category: Adenylosuccinate synthase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: Chemla, P | + | [[Category: Chemla, P]] |
| - | [[Category: Cowan-Jacob, S W | + | [[Category: Cowan-Jacob, S W]] |
| - | [[Category: Fonne-Pfister, R | + | [[Category: Fonne-Pfister, R]] |
| - | [[Category: Gohda, K | + | [[Category: Gohda, K]] |
| - | [[Category: Hanessian, S | + | [[Category: Hanessian, S]] |
| - | [[Category: Lu, P P | + | [[Category: Lu, P P]] |
| - | [[Category: Prade, L | + | [[Category: Prade, L]] |
| - | [[Category: Sanceau, J Y | + | [[Category: Sanceau, J Y]] |
[[Category: Gtp-binding]] | [[Category: Gtp-binding]] | ||
[[Category: Gtp-hydrolysing enzyme]] | [[Category: Gtp-hydrolysing enzyme]] | ||
Revision as of 23:43, 24 December 2014
DESIGN, SYNTHESIS, AND X-RAY CRYSTAL STRUCTURE OF AN ENZYME BOUND BISUBSTRATE HYBRID INHIBITOR OF ADENYLOSUCCINATE SYNTHETASE
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