1nh0
From Proteopedia
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|PDB= 1nh0 |SIZE=350|CAPTION= <scene name='initialview01'>1nh0</scene>, resolution 1.03Å | |PDB= 1nh0 |SIZE=350|CAPTION= <scene name='initialview01'>1nh0</scene>, resolution 1.03Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=KI2:3-BENZYLOXYCARBONYLAMINO-2-HYDROXY-4-PHENYL-BUTYRIC+ACID'>KI2</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/HIV-1_retropepsin HIV-1 retropepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.16 3.4.23.16] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/HIV-1_retropepsin HIV-1 retropepsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.16 3.4.23.16] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1nh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1nh0 OCA], [http://www.ebi.ac.uk/pdbsum/1nh0 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1nh0 RCSB]</span> | ||
}} | }} | ||
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[[Category: Sedlacek, J.]] | [[Category: Sedlacek, J.]] | ||
[[Category: Soucek, M.]] | [[Category: Soucek, M.]] | ||
| - | [[Category: BME]] | ||
| - | [[Category: NH2]] | ||
| - | [[Category: SO4]] | ||
[[Category: aspartyl protease]] | [[Category: aspartyl protease]] | ||
[[Category: human immunodeficiency virus]] | [[Category: human immunodeficiency virus]] | ||
[[Category: inhibitor design]] | [[Category: inhibitor design]] | ||
| - | ''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 22:30:16 2008'' |
Revision as of 19:30, 30 March 2008
| |||||||
| , resolution 1.03Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Activity: | HIV-1 retropepsin, with EC number 3.4.23.16 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
1.03 A structure of HIV-1 protease: inhibitor binding inside and outside the active site
Overview
The X-ray structure of a complex of HIV-1 protease (PR) with a phenylnorstatine inhibitor Z-Pns-Phe-Glu-Glu-NH(2) has been determined at 1.03 A, the highest resolution so far reported for any HIV PR complex. The inhibitor shows subnanomolar K(i) values for both the wild-type PR and the variant representing one of the most common mutations linked to resistance development. The structure comprising the phenylnorstatine moiety of (2R,3S)-chirality displays a unique pattern of hydrogen bonding to the two catalytic aspartate residues. This high resolution makes it possible to assess the donor and acceptor relations of this hydrogen bonding and to indicate a proton shared by the two catalytic residues. A structural mechanism for the unimpaired inhibition of the protease Val82Ala mutant is also suggested, based on energy calculations and analyses.
About this Structure
1NH0 is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
Reference
A phenylnorstatine inhibitor binding to HIV-1 protease: geometry, protonation, and subsite-pocket interactions analyzed at atomic resolution., Brynda J, Rezacova P, Fabry M, Horejsi M, Stouracova R, Sedlacek J, Soucek M, Hradilek M, Lepsik M, Konvalinka J, J Med Chem. 2004 Apr 8;47(8):2030-6. PMID:15056001
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