1epq: Difference between revisions
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|PDB= 1epq |SIZE=350|CAPTION= <scene name='initialview01'>1epq</scene>, resolution 1.9Å | |PDB= 1epq |SIZE=350|CAPTION= <scene name='initialview01'>1epq</scene>, resolution 1.9Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SOT:N-HYDROSULFONYLMORPHOLINE'>SOT</scene> | |LIGAND= <scene name='pdbligand=SCC:THIOETHYL+GROUP'>SCC</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=SOT:N-HYDROSULFONYLMORPHOLINE'>SOT</scene>, <scene name='pdbligand=XAO:CYCLOHEXYLMETHYL-2,3-DIHYDROXY-5-METHYL-HEXYLAMIDE'>XAO</scene> | ||
|ACTIVITY= [http://en.wikipedia.org/wiki/Endothiapepsin Endothiapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.22 3.4.23.22] | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Endothiapepsin Endothiapepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.22 3.4.23.22] </span> | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1epq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1epq OCA], [http://www.ebi.ac.uk/pdbsum/1epq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1epq RCSB]</span> | |||
}} | }} | ||
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[[Category: Cooper, J B.]] | [[Category: Cooper, J B.]] | ||
[[Category: Dealwis, C.]] | [[Category: Dealwis, C.]] | ||
[[Category: hydrolase(acid proteinase)]] | [[Category: hydrolase(acid proteinase)]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:07:17 2008'' | ||
Revision as of 20:07, 30 March 2008
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| , resolution 1.9Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | Endothiapepsin, with EC number 3.4.23.22 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ANALYSES OF LIGAND BINDING IN FIVE ENDOTHIAPEPSIN CRYSTAL COMPLEXES AND THEIR USE IN THE DESIGN AND EVALUATION OF NOVEL RENIN INHIBITORS
OverviewOverview
Five renin inhibitors were cocrystallized with endothiapepsin, a fungal enzyme homologous to renin. Crystal structures of inhibitor-bound complexes have provided invaluable insight regarding the three-dimensional structure of the aspartic proteinase family of enzymes, as well as the steric and polar interactions that occur between the proteins and the bound ligands. Beyond this, subtleties of binding have been revealed, including multiple subsite binding modes and subsite interdependencies. This information has been applied in the design of novel potent renin inhibitors and in the understanding of structure-activity relationships and enzyme selectivities.
About this StructureAbout this Structure
1EPQ is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
ReferenceReference
Analyses of ligand binding in five endothiapepsin crystal complexes and their use in the design and evaluation of novel renin inhibitors., Lunney EA, Hamilton HW, Hodges JC, Kaltenbronn JS, Repine JT, Badasso M, Cooper JB, Dealwis C, Wallace BA, Lowther WT, et al., J Med Chem. 1993 Nov 26;36(24):3809-20. PMID:8254610
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