5frb - Revision history

OCA at 13:19, 26 July 2023

2023-07-26T13:19:56Z

←Older revision		Revision as of 13:19, 26 July 2023
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	==Crystal structure of sterol 14-alpha demethylase (CYP51B) from a pathogenic filamentous fungus Aspergillus fumigatus in complex with a tetrazole-based inhibitor VT-1598==		==Crystal structure of sterol 14-alpha demethylase (CYP51B) from a pathogenic filamentous fungus Aspergillus fumigatus in complex with a tetrazole-based inhibitor VT-1598==
-	<StructureSection load='5frb' size='340' side='right' caption='[[5frb]], [[Resolution\|resolution]] 2.99Å' scene=''>	+	<StructureSection load='5frb' size='340' side='right'caption='[[5frb]], [[Resolution\|resolution]] 2.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5frb]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Aspfm Aspfm~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FRB OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=5FRB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5frb]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Aspergillus_fumigatus Aspergillus fumigatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FRB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5FRB FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=VT2:(R)-4-((4-((6-(2-(2,4-DIFLUOROPHENYL)-1,1-DIFLUORO-2-HYDROXY-3-(1H-TETRAZOL-1-YL)PROPYL)PYRIDIN-3-YL)ETHYNYL)PHENOXY)METHYL)BENZONITRILE'>VT2</scene~~></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 2.99Å</td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERG 11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=746128 ASPFM])</td></tr>~~	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=VT2:(R)-4-((4-((6-(2-(2,4-DIFLUOROPHENYL)-1,1-DIFLUORO-2-HYDROXY-3-(1H-TETRAZOL-1-YL)PROPYL)PYRIDIN-3-YL)ETHYNYL)PHENOXY)METHYL)BENZONITRILE'>VT2</scene></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sterol_14-demethylase Sterol 14-demethylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.70 1.14.13.70] </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=5frb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5frb OCA], [https://pdbe.org/5frb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5frb RCSB], [https://www.ebi.ac.uk/pdbsum/5frb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5frb ProSAT]</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=5frb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5frb OCA], [~~http~~://pdbe.org/5frb PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=5frb RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/5frb PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=5frb ProSAT]</span></td></tr>	+
	</table>		</table>
		+	== Function ==
		+	[https://www.uniprot.org/uniprot/CP51B_ASPFU CP51B_ASPFU] Sterol 14-alpha demethylase; part of the third module of ergosterol biosynthesis pathway that includes the late steps of the pathway (PubMed:18191972, PubMed:26459890, PubMed:29439966, PubMed:9184358). Demethylates eburicol to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol (PubMed:18191972, PubMed:26459890, PubMed:29439966, PubMed:9184358). The third module or late pathway involves the ergosterol synthesis itself through consecutive reactions that mainly occur in the endoplasmic reticulum (ER) membrane. Firstly, the squalene synthase erg9 catalyzes the condensation of 2 farnesyl pyrophosphate moieties to form squalene, which is the precursor of all steroids. Squalene synthase is crucial for balancing the incorporation of farnesyl diphosphate (FPP) into sterol and nonsterol isoprene synthesis. Secondly, squalene is converted into lanosterol by the consecutive action of the squalene epoxidase erg1 and the lanosterol synthase erg7. Then, the delta(24)-sterol C-methyltransferase erg6 methylates lanosterol at C-24 to produce eburicol. Eburicol is the substrate of the sterol 14-alpha demethylase encoded by cyp51A and cyp51B, to yield 4,4,24-trimethyl ergosta-8,14,24(28)-trienol. The C-14 reductase erg24 then reduces the C14=C15 double bond which leads to 4,4-dimethylfecosterol. A sequence of further demethylations at C-4, involving the C-4 demethylation complex containing the C-4 methylsterol oxidases erg25A or erg25B, the sterol-4-alpha-carboxylate 3-dehydrogenase erg26 and the 3-keto-steroid reductase erg27, leads to the production of fecosterol via 4-methylfecosterol. The C-8 sterol isomerase erg2 then catalyzes the reaction which results in unsaturation at C-7 in the B ring of sterols and thus converts fecosterol to episterol. The sterol-C5-desaturase erg3B then catalyzes the introduction of a C-5 double bond in the B ring to produce 5-dehydroepisterol. The 2 other sterol-C5-desaturases, erg3A and erg3C, seem to be less important in ergosterol biosynthesis. The C-22 sterol desaturase erg5 further converts 5-dehydroepisterol into ergosta-5,7,22,24(28)-tetraen-3beta-ol by forming the C-22(23) double bond in the sterol side chain. Finally, ergosta-5,7,22,24(28)-tetraen-3beta-ol is substrate of the C-24(28) sterol reductases erg4A and erg4B to produce ergosterol. Possible alternative sterol biosynthetic pathways might exist from fecosterol to ergosterol, depending on the activities of the erg3 isoforms (PubMed:16110826, PubMed:18191972) (Probable).<ref>PMID:18191972</ref> <ref>PMID:26459890</ref> <ref>PMID:29439966</ref> <ref>PMID:9184358</ref> <ref>PMID:16110826</ref> <ref>PMID:18191972</ref> As a target of azole drugs, plays a crucial role in azole susceptibility.<ref>PMID:12543662</ref> <ref>PMID:26269599</ref> <ref>PMID:28461309</ref> <ref>PMID:29894182</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 22:		Line 23:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Aspfm~~]]	+	[[Category: Aspergillus fumigatus]]
-	[[Category: ~~Sterol 14-demethylase~~]]	+	[[Category: Large Structures]]
-	[[Category: Hargrove~~, T Y~~]]	+	[[Category: Hargrove TY]]
-	[[Category: Lepesheva~~, G I~~]]	+	[[Category: Lepesheva GI]]
-	[[Category: Wawrzak, Z]]	+	[[Category: Wawrzak Z]]
-	~~[[Category: Cytochrome p450]]~~	+
-	~~[[Category: Cytochrome p450 fold]]~~	+
-	~~[[Category: Endoplasmic reticulum membrane]]~~	+
-	~~[[Category: Eukaryotic membrane]]~~	+
-	~~[[Category: Heme]]~~	+
-	~~[[Category: Monooxygenase]]~~	+
-	~~[[Category: Oxidoreductase]]~~	+
-	~~[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]~~	+
-	~~[[Category: Sterol biosynthesis~~]]	+

OCA at 07:56, 16 November 2017

2017-11-16T07:56:23Z

←Older revision		Revision as of 07:56, 16 November 2017
Line 3:		Line 3:
	<StructureSection load='5frb' size='340' side='right' caption='[[5frb]], [[Resolution\|resolution]] 2.99Å' scene=''>		<StructureSection load='5frb' size='340' side='right' caption='[[5frb]], [[Resolution\|resolution]] 2.99Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[5frb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FRB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FRB FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[5frb]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Aspfm Aspfm]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FRB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FRB FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=VT2:(R)-4-((4-((6-(2-(2,4-DIFLUOROPHENYL)-1,1-DIFLUORO-2-HYDROXY-3-(1H-TETRAZOL-1-YL)PROPYL)PYRIDIN-3-YL)ETHYNYL)PHENOXY)METHYL)BENZONITRILE'>VT2</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=VT2:(R)-4-((4-((6-(2-(2,4-DIFLUOROPHENYL)-1,1-DIFLUORO-2-HYDROXY-3-(1H-TETRAZOL-1-YL)PROPYL)PYRIDIN-3-YL)ETHYNYL)PHENOXY)METHYL)BENZONITRILE'>VT2</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">ERG 11 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=746128 ASPFM])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sterol_14-demethylase Sterol 14-demethylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.70 1.14.13.70] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sterol_14-demethylase Sterol 14-demethylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.70 1.14.13.70] </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=5frb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5frb OCA], [http://pdbe.org/5frb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5frb RCSB], [http://www.ebi.ac.uk/pdbsum/5frb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5frb ProSAT]</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=5frb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5frb OCA], [http://pdbe.org/5frb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5frb RCSB], [http://www.ebi.ac.uk/pdbsum/5frb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5frb ProSAT]</span></td></tr>
Line 21:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
		+	[[Category: Aspfm]]
	[[Category: Sterol 14-demethylase]]		[[Category: Sterol 14-demethylase]]
	[[Category: Hargrove, T Y]]		[[Category: Hargrove, T Y]]

OCA at 09:01, 17 May 2017

2017-05-17T09:01:59Z

←Older revision		Revision as of 09:01, 17 May 2017
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	<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=5frb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5frb OCA], [http://pdbe.org/5frb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5frb RCSB], [http://www.ebi.ac.uk/pdbsum/5frb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5frb ProSAT]</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=5frb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5frb OCA], [http://pdbe.org/5frb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5frb RCSB], [http://www.ebi.ac.uk/pdbsum/5frb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5frb ProSAT]</span></td></tr>
	</table>		</table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Within the past decades, the incidence and complexity of human fungal infections have increased, and therefore the need for safer and more efficient, broad-spectrum antifungal agents is high. Herein, we characterize the new tetrazole-based drug candidate VT-1598 as an inhibitor of sterol 14alpha-demethylase (CYP51B) from the filamentous fungi Aspergillus fumigatus VT-1598 displayed a high binding affinity to the enzyme in solution (with the Kd of 13+/-1 nM) and in the reconstituted enzymatic reaction revealed the inhibitory potency stronger than the potencies of all other simultaneously tested antifungal drugs, including fluconazole, voriconazole, ketoconazole, and posaconazole. The X-ray structure of the VT-1598/A. fumigatus CYP51 complex has been determined depicting the distinctive binding mode of the inhibitor in the enzyme active site and suggesting the molecular basis of the improved drug potency and broad-spectrum antifungal activity. These data show the formation of an optimized hydrogen bond between the phenoxymethyl oxygen of VT-1598 and the imidazole ring nitrogen of His-374, the CYP51 residue that is highly conserved across fungal pathogens and fungi-specific. Comparative structural analysis of A. fumigatus CYP51/voriconazole and C. albicans CYP51/VT-1161 complexes supports the role of H-bonding in fungal CYP51-inhibitor complexes, and emphasizes the importance of an optimal distance between this interaction and the inhibitor-heme iron interaction. Cellular experiments using two A. fumigatus strains (32820 and 1022) displayed direct correlation between the effects of the drugs on the CYP51B activity and fungal growth inhibition, indicating the noteworthy anti-A. fumigatus potency of VT-1598 and confirming its promise as a broad-spectrum antifungal agent.
		+
		+	Crystal structure of the new investigational drug candidate VT-1598 in complex with Aspergillus fumigatus sterol 14alpha-demethylase provides insights into its broad-spectrum antifungal activity.,Hargrove TY, Garvey EP, Hoekstra WJ, Yates CM, Wawrzak Z, Rachakonda G, Villalta F, Lepesheva GI Antimicrob Agents Chemother. 2017 May 1. pii: AAC.00570-17. doi:, 10.1128/AAC.00570-17. PMID:28461309<ref>PMID:28461309</ref>
		+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>
		+	<div class="pdbe-citations 5frb" style="background-color:#fffaf0;"></div>
		+	== References ==
		+	<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 13:56, 27 April 2017

2017-04-27T13:56:41Z

←Older revision		Revision as of 13:56, 27 April 2017
Line 1:		Line 1:
-	'''Unreleased structure'''

-	~~The entry 5frb is ON HOLD until Apr 16 2018~~	+	==Crystal structure of sterol 14-alpha demethylase (CYP51B) from a pathogenic filamentous fungus Aspergillus fumigatus in complex with a tetrazole-based inhibitor VT-1598==
-		+	<StructureSection load='5frb' size='340' side='right' caption='[[5frb]], [[Resolution\|resolution]] 2.99Å' scene=''>
-	~~Authors: Hargrove, T.Y., Wawrzak, Z., Lepesheva, G.I.~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[5frb]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5FRB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5FRB FirstGlance]. <br>
-	~~Description:~~ Crystal structure of sterol 14-alpha demethylase (CYP51B) from a pathogenic filamentous fungus Aspergillus fumigatus in complex with a tetrazole-based inhibitor VT-1598	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HEM:PROTOPORPHYRIN+IX+CONTAINING+FE'>HEM</scene>, <scene name='pdbligand=VT2:(R)-4-((4-((6-(2-(2,4-DIFLUOROPHENYL)-1,1-DIFLUORO-2-HYDROXY-3-(1H-TETRAZOL-1-YL)PROPYL)PYRIDIN-3-YL)ETHYNYL)PHENOXY)METHYL)BENZONITRILE'>VT2</scene></td></tr>
-	[[Category: ~~Unreleased Structures~~]]	+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Sterol_14-demethylase Sterol 14-demethylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.14.13.70 1.14.13.70] </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=5frb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5frb OCA], [http://pdbe.org/5frb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5frb RCSB], [http://www.ebi.ac.uk/pdbsum/5frb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5frb ProSAT]</span></td></tr>
		+	</table>
		+	__TOC__
		+	</StructureSection>
		+	[[Category: Sterol 14-demethylase]]
		+	[[Category: Hargrove, T Y]]
		+	[[Category: Lepesheva, G I]]
	[[Category: Wawrzak, Z]]		[[Category: Wawrzak, Z]]
-	[[Category: ~~Hargrove, T.Y~~]]	+	[[Category: Cytochrome p450]]
-	[[Category: ~~Lepesheva, G.I~~]]	+	[[Category: Cytochrome p450 fold]]
		+	[[Category: Endoplasmic reticulum membrane]]
		+	[[Category: Eukaryotic membrane]]
		+	[[Category: Heme]]
		+	[[Category: Monooxygenase]]
		+	[[Category: Oxidoreductase]]
		+	[[Category: Oxidoreductase-oxidoreductase inhibitor complex]]
		+	[[Category: Sterol biosynthesis]]

OCA at 07:33, 29 March 2017

2017-03-29T07:33:30Z

←Older revision		Revision as of 07:33, 29 March 2017
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5frb is ON HOLD until ~~Dec~~ 16 ~~2017~~	+	The entry 5frb is ON HOLD until Apr 16 2018

	Authors: Hargrove, T.Y., Wawrzak, Z., Lepesheva, G.I.		Authors: Hargrove, T.Y., Wawrzak, Z., Lepesheva, G.I.

OCA at 18:19, 30 December 2015

2015-12-30T18:19:25Z

←Older revision		Revision as of 18:19, 30 December 2015
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 5frb is ON HOLD until ~~sometime in the future~~	+	The entry 5frb is ON HOLD until Dec 16 2017

	Authors: Hargrove, T.Y., Wawrzak, Z., Lepesheva, G.I.		Authors: Hargrove, T.Y., Wawrzak, Z., Lepesheva, G.I.

OCA: Protected "5frb" [edit=sysop:move=sysop]

2015-12-23T11:51:30Z

Protected "5frb" [edit=sysop:move=sysop]

←Older revision

Revision as of 11:51, 23 December 2015

OCA: New page: '''Unreleased structure''' The entry 5frb is ON HOLD until sometime in the future Authors: Hargrove, T.Y., Wawrzak, Z., Lepesheva, G.I. Description: Crystal structure of sterol 14-alph...

2015-12-23T11:51:29Z

New page: '''Unreleased structure''' The entry 5frb is ON HOLD until sometime in the future Authors: Hargrove, T.Y., Wawrzak, Z., Lepesheva, G.I. Description: Crystal structure of sterol 14-alph...

New page

'''Unreleased structure'''

The entry 5frb is ON HOLD until sometime in the future

Authors: Hargrove, T.Y., Wawrzak, Z., Lepesheva, G.I.

Description: Crystal structure of sterol 14-alpha demethylase (CYP51B) from a pathogenic filamentous fungus Aspergillus fumigatus in complex with a tetrazole-based inhibitor VT-1598
[[Category: Unreleased Structures]]
[[Category: Wawrzak, Z]]
[[Category: Hargrove, T.Y]]
[[Category: Lepesheva, G.I]]