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1atl
From Proteopedia
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==Structural interaction of natural and synthetic inhibitors with the VENOM METALLOPROTEINASE, ATROLYSIN C (FORM-D)== | ==Structural interaction of natural and synthetic inhibitors with the VENOM METALLOPROTEINASE, ATROLYSIN C (FORM-D)== | ||
<StructureSection load='1atl' size='340' side='right' caption='[[1atl]], [[Resolution|resolution]] 1.80Å' scene=''> | <StructureSection load='1atl' size='340' side='right' caption='[[1atl]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0QI:O-METHYL-N-[(2S)-4-METHYL-2-(SULFANYLMETHYL)PENTANOYL]-L-TYROSINE'>0QI</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0QI:O-METHYL-N-[(2S)-4-METHYL-2-(SULFANYLMETHYL)PENTANOYL]-L-TYROSINE'>0QI</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Atrolysin_C Atrolysin C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.42 3.4.24.42] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Atrolysin_C Atrolysin C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.42 3.4.24.42] </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=1atl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1atl OCA], [http://pdbe.org/1atl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1atl RCSB], [http://www.ebi.ac.uk/pdbsum/1atl 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=1atl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1atl OCA], [http://pdbe.org/1atl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1atl RCSB], [http://www.ebi.ac.uk/pdbsum/1atl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1atl ProSAT]</span></td></tr> |
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 10:45, 15 November 2017
Structural interaction of natural and synthetic inhibitors with the VENOM METALLOPROTEINASE, ATROLYSIN C (FORM-D)
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