1pda
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1pda]] 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=1PDA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PDA FirstGlance]. <br> | <table><tr><td colspan='2'>[[1pda]] 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=1PDA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PDA FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=DPM:3-[5-{[3-(2-CARBOXYETHYL)-4-(CARBOXYMETHYL)-5-METHYL-1H-PYRROL-2-YL]METHYL}-4-(CARBOXYMETHYL)-1H-PYRROL-3-YL]PROPANOIC+ACID'>DPM</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=DPM:3-[5-{[3-(2-CARBOXYETHYL)-4-(CARBOXYMETHYL)-5-METHYL-1H-PYRROL-2-YL]METHYL}-4-(CARBOXYMETHYL)-1H-PYRROL-3-YL]PROPANOIC+ACID'>DPM</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydroxymethylbilane_synthase Hydroxymethylbilane synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.61 2.5.1.61] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Hydroxymethylbilane_synthase Hydroxymethylbilane synthase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.5.1.61 2.5.1.61] </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=1pda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pda OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pda RCSB], [http://www.ebi.ac.uk/pdbsum/1pda 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=1pda FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pda OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pda RCSB], [http://www.ebi.ac.uk/pdbsum/1pda PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/HEM3_ECOLI HEM3_ECOLI]] Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps.[HAMAP-Rule:MF_00260] | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Hydroxymethylbilane synthase]] | [[Category: Hydroxymethylbilane synthase]] | ||
| - | [[Category: Blundell, T L | + | [[Category: Blundell, T L]] |
| - | [[Category: Brownlie, P D | + | [[Category: Brownlie, P D]] |
| - | [[Category: Cooper, J B | + | [[Category: Cooper, J B]] |
| - | [[Category: Jordan, P M | + | [[Category: Jordan, P M]] |
| - | [[Category: Lambert, R | + | [[Category: Lambert, R]] |
| - | [[Category: Louie, G V | + | [[Category: Louie, G V]] |
| - | [[Category: Warren, M J | + | [[Category: Warren, M J]] |
| - | [[Category: Wood, S P | + | [[Category: Wood, S P]] |
| - | [[Category: Woodcock, S C | + | [[Category: Woodcock, S C]] |
[[Category: Porphyrin]] | [[Category: Porphyrin]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 20:26, 25 December 2014
STRUCTURE OF PORPHOBILINOGEN DEAMINASE REVEALS A FLEXIBLE MULTIDOMAIN POLYMERASE WITH A SINGLE CATALYTIC SITE
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