1bma: Difference between revisions

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<StructureSection load='1bma' size='340' side='right'caption='[[1bma]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
<StructureSection load='1bma' size='340' side='right'caption='[[1bma]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1bma]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BMA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BMA FirstGlance]. <br>
<table><tr><td colspan='2'>[[1bma]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BMA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BMA FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0QH:(1R)-1-BENZYL-1-METHYL-1-(2-{[4-(1-METHYLETHYL)PHENYL]AMINO}-2-OXOETHYL)-2-{(2S)-4-METHYL-2-[(TRIFLUOROACETYL)AMINO]PENTANOYL}DIAZANIUM'>0QH</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0QH:(1R)-1-BENZYL-1-METHYL-1-(2-{[4-(1-METHYLETHYL)PHENYL]AMINO}-2-OXOETHYL)-2-{(2S)-4-METHYL-2-[(TRIFLUOROACETYL)AMINO]PENTANOYL}DIAZANIUM'>0QH</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] </span></td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Pancreatic_elastase Pancreatic elastase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.36 3.4.21.36] </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=1bma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bma OCA], [http://pdbe.org/1bma PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bma RCSB], [http://www.ebi.ac.uk/pdbsum/1bma PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1bma ProSAT]</span></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=1bma FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bma OCA], [https://pdbe.org/1bma PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bma RCSB], [https://www.ebi.ac.uk/pdbsum/1bma PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bma ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CELA1_PIG CELA1_PIG]] Acts upon elastin.  
[[https://www.uniprot.org/uniprot/CELA1_PIG CELA1_PIG]] Acts upon elastin.  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]

Revision as of 18:08, 2 June 2021

BENZYL METHYL AMINIMIDE INHIBITOR COMPLEXED TO PORCINE PANCREATIC ELASTASEBENZYL METHYL AMINIMIDE INHIBITOR COMPLEXED TO PORCINE PANCREATIC ELASTASE

Structural highlights

1bma is a 1 chain structure with sequence from Sus scrofa. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Activity:Pancreatic elastase, with EC number 3.4.21.36
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CELA1_PIG] Acts upon elastin.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The crystal structure of an aminimide analog of a dipeptide inhibitor of porcine pancreatic elastase bound to its target serine protease has been solved. The peptidomimetic molecule binds in the same fashion as the class of dipeptides from which it was derived, making similar interactions with the subsites on the elastase surface. Because aminimides are readily synthesized from a wide variety of starting materials, they form the basis for a combinatorial chemistry approach to rational drug design.

Interaction of a peptidomimetic aminimide inhibitor with elastase.,Peisach E, Casebier D, Gallion SL, Furth P, Petsko GA, Hogan JC Jr, Ringe D Science. 1995 Jul 7;269(5220):66-9. PMID:7604279[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Peisach E, Casebier D, Gallion SL, Furth P, Petsko GA, Hogan JC Jr, Ringe D. Interaction of a peptidomimetic aminimide inhibitor with elastase. Science. 1995 Jul 7;269(5220):66-9. PMID:7604279

1bma, resolution 1.80Å

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