2ahd: Difference between revisions

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== Structural highlights ==

<table><tr><td colspan='2'>[[2ahd]] is a 4 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AHD OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=2AHD FirstGlance]. <br>

<table><tr><td colspan='2'>[[2ahd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AHD FirstGlance]. <br>

</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=2ahd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahd OCA], [~~http~~://pdbe.org/2ahd PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=2ahd RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/2ahd PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=2ahd ProSAT]</span></td></tr>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ahd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahd OCA], [https://pdbe.org/2ahd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ahd RCSB], [https://www.ebi.ac.uk/pdbsum/2ahd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ahd ProSAT]</span></td></tr>

</table>

== Function ==

[[~~http~~://www.uniprot.org/uniprot/P936_METJA P936_METJA]] Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown.

[[https://www.uniprot.org/uniprot/P936_METJA P936_METJA]] Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown.

== Evolutionary Conservation ==

[[Image:Consurf_key_small.gif|200px|right]]

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 <StructureSection load='2ahd' size='340' side='right'caption='[[2ahd]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ahd]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AHD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2AHD FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ahd]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_43067 Atcc 43067]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AHD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2AHD FirstGlance]. <br>
-</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=2ahd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahd OCA], [http://pdbe.org/2ahd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2ahd RCSB], [http://www.ebi.ac.uk/pdbsum/2ahd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2ahd ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ahd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ahd OCA], [https://pdbe.org/2ahd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ahd RCSB], [https://www.ebi.ac.uk/pdbsum/2ahd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ahd ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/P936_METJA P936_METJA]] Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown.
+[[https://www.uniprot.org/uniprot/P936_METJA P936_METJA]] Shows phosphodiesterase activity, hydrolyzing phosphodiesters bonds in the artificial chromogenic substrates bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p-nitrophenylphosphorylcholine (pNPPC). No catalytic activity was found toward cAMP or cGMP, nucleotides or phospholipase substrates such as phosphatidylcholine. The physiological substrate is unknown.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]