2i5b
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2i5b]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I5B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2I5B FirstGlance]. <br> | <table><tr><td colspan='2'>[[2i5b]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2I5B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2I5B FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">thiD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">thiD ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1423 Bacillus subtilis])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphomethylpyrimidine_kinase Phosphomethylpyrimidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.7 2.7.4.7] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphomethylpyrimidine_kinase Phosphomethylpyrimidine kinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.4.7 2.7.4.7] </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=2i5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i5b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2i5b RCSB], [http://www.ebi.ac.uk/pdbsum/2i5b 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=2i5b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2i5b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2i5b RCSB], [http://www.ebi.ac.uk/pdbsum/2i5b PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/THID_BACSU THID_BACSU]] Catalyzes the phosphorylation of hydroxymethylpyrimidine phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. Shows no activity with pyridoxal, pyridoxamine or pyridoxine. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Phosphomethylpyrimidine kinase]] | [[Category: Phosphomethylpyrimidine kinase]] | ||
| - | [[Category: Das, S K | + | [[Category: Das, S K]] |
| - | [[Category: Newman, J A | + | [[Category: Newman, J A]] |
| - | [[Category: Rice, D W | + | [[Category: Rice, D W]] |
| - | [[Category: Sedelnikova, S E | + | [[Category: Sedelnikova, S E]] |
[[Category: Adp complex]] | [[Category: Adp complex]] | ||
[[Category: Pdxk]] | [[Category: Pdxk]] | ||
Revision as of 14:59, 24 December 2014
The crystal structure of an ADP complex of Bacillus subtilis pyridoxal kinase provides evidence for the parralel emergence of enzyme activity during evolution
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