1q1k
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1q1k]] 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=1Q1K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q1K FirstGlance]. <br> | <table><tr><td colspan='2'>[[1q1k]] 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=1Q1K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1Q1K FirstGlance]. <br> | ||
- | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRT:PHOSPHORIBOSYL+ATP'>PRT</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PRT:PHOSPHORIBOSYL+ATP'>PRT</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</scene></td></tr> |
- | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HISG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HISG ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli])</td></tr> |
- | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ATP_phosphoribosyltransferase ATP phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.17 2.4.2.17] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ATP_phosphoribosyltransferase ATP phosphoribosyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.4.2.17 2.4.2.17] </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=1q1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q1k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1q1k RCSB], [http://www.ebi.ac.uk/pdbsum/1q1k 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=1q1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q1k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1q1k RCSB], [http://www.ebi.ac.uk/pdbsum/1q1k PDBsum]</span></td></tr> |
- | <table> | + | </table> |
+ | == Function == | ||
+ | [[http://www.uniprot.org/uniprot/HIS1_ECOLI HIS1_ECOLI]] Catalyzes the condensation of ATP and 5-phosphoribose 1-diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a crucial role in the pathway because the rate of histidine biosynthesis seems to be controlled primarily by regulation of HisG enzymatic activity.[HAMAP-Rule:MF_00079] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: ATP phosphoribosyltransferase]] | [[Category: ATP phosphoribosyltransferase]] | ||
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
- | [[Category: Coggins, J R | + | [[Category: Coggins, J R]] |
- | [[Category: Lapthorn, A J | + | [[Category: Lapthorn, A J]] |
- | [[Category: Lohkamp, B | + | [[Category: Lohkamp, B]] |
- | [[Category: McDermott, G | + | [[Category: McDermott, G]] |
[[Category: Histidine biosynthesis]] | [[Category: Histidine biosynthesis]] | ||
[[Category: Pr-atp inhibition]] | [[Category: Pr-atp inhibition]] | ||
[[Category: Prpp binding]] | [[Category: Prpp binding]] | ||
[[Category: Transferase]] | [[Category: Transferase]] |
Revision as of 22:15, 25 December 2014
Structure of ATP-phosphoribosyltransferase from E. coli complexed with PR-ATP
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