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3fnm
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[3fnm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FNM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FNM FirstGlance]. <br> | <table><tr><td colspan='2'>[[3fnm]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Helicobacter_pylori Helicobacter pylori]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FNM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3FNM FirstGlance]. <br> | ||
| - | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AVN:(2S)-AMINO[(5S)-3-CHLORO-4,5-DIHYDROISOXAZOL-5-YL]ACETIC+ACID'>AVN</scene>< | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=AVN:(2S)-AMINO[(5S)-3-CHLORO-4,5-DIHYDROISOXAZOL-5-YL]ACETIC+ACID'>AVN</scene></td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nqo|2nqo]], [[2qmg|2qmg]]</td></tr> | + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2nqo|2nqo]], [[2qmg|2qmg]]</td></tr> |
| - | <tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP_1118 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori])</td></tr> | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">HP_1118 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=210 Helicobacter pylori])</td></tr> |
| - | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Gamma-glutamyltransferase Gamma-glutamyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.2 2.3.2.2] </span></td></tr> | + | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Gamma-glutamyltransferase Gamma-glutamyltransferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.2 2.3.2.2] </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=3fnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fnm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fnm RCSB], [http://www.ebi.ac.uk/pdbsum/3fnm 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=3fnm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fnm OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3fnm RCSB], [http://www.ebi.ac.uk/pdbsum/3fnm PDBsum]</span></td></tr> |
| - | <table> | + | </table> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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Crystal Structure of Acivicin-Inhibited gamma-Glutamyltranspeptidase Reveals Critical Roles for Its C-Terminus in Autoprocessing and Catalysis (dagger) (double dagger).,Williams K, Cullati S, Sand A, Biterova EI, Barycki JJ Biochemistry. 2009 Mar 24;48(11):2459-67. PMID:19256527<ref>PMID:19256527</ref> | Crystal Structure of Acivicin-Inhibited gamma-Glutamyltranspeptidase Reveals Critical Roles for Its C-Terminus in Autoprocessing and Catalysis (dagger) (double dagger).,Williams K, Cullati S, Sand A, Biterova EI, Barycki JJ Biochemistry. 2009 Mar 24;48(11):2459-67. PMID:19256527<ref>PMID:19256527</ref> | ||
| - | From | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
</div> | </div> | ||
== References == | == References == | ||
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[[Category: Gamma-glutamyltransferase]] | [[Category: Gamma-glutamyltransferase]] | ||
[[Category: Helicobacter pylori]] | [[Category: Helicobacter pylori]] | ||
| - | [[Category: Barycki, J J | + | [[Category: Barycki, J J]] |
| - | [[Category: Biterova, E I | + | [[Category: Biterova, E I]] |
| - | [[Category: Cullati, S | + | [[Category: Cullati, S]] |
| - | [[Category: Sand, A | + | [[Category: Sand, A]] |
| - | [[Category: Williams, K | + | [[Category: Williams, K]] |
[[Category: Glutamyltranspeptidase]] | [[Category: Glutamyltranspeptidase]] | ||
[[Category: Ntn-hydrolase]] | [[Category: Ntn-hydrolase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 23:01, 3 January 2015
Crystal structure of acivicin-inhibited gamma-glutamyltranspeptidase reveals critical roles for its C-terminus in autoprocessing and catalysis
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