This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1bhs

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (06:36, 7 February 2024) (edit) (undo)
 
(23 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1bhs.gif|left|200px]]<br />
 
-
<applet load="1bhs" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="1bhs, resolution 2.20&Aring;" />
 
-
'''HUMAN ESTROGENIC 17BETA-HYDROXYSTEROID DEHYDROGENASE'''<br />
 
-
==Overview==
+
==HUMAN ESTROGENIC 17BETA-HYDROXYSTEROID DEHYDROGENASE==
-
BACKGROUND: The principal human estrogen, 17 beta-estradiol, is a potent, stimulator of certain endocrine-dependent forms of breast cancer. Because, human estrogenic 17 beta-hydroxysteroid dehydrogenase (type I 17 beta-HSD), catalyzes the last step in the biosynthesis of 17 beta-estradiol from the, less potent estrogen, estrone, it is an attractive target for the design, of inhibitors of estrogen production and tumor growth. This human enzyme, shares less than 15% sequence identity with a bacterial 3 alpha,20, beta-HSD, for which the three-dimensional structure is known. The amino, acid sequence of 17 beta-HSD also differs from that of bacterial 3, alpha,20 beta-HSD by two insertions (of 11 and 14 residues) and 52, additional residues at the C terminus. RESULTS: The 2.20 A resolution, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?7663947 (full description)]]
+
<StructureSection load='1bhs' size='340' side='right'caption='[[1bhs]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[1bhs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BHS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BHS FirstGlance]. <br>
 +
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</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=1bhs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bhs OCA], [https://pdbe.org/1bhs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bhs RCSB], [https://www.ebi.ac.uk/pdbsum/1bhs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bhs ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/DHB1_HUMAN DHB1_HUMAN] Favors the reduction of estrogens and androgens. Also has 20-alpha-HSD activity. Uses preferentially NADH.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bh/1bhs_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1bhs ConSurf].
 +
<div style="clear:both"></div>
-
==About this Structure==
+
==See Also==
-
1BHS is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]]. Active as [[http://en.wikipedia.org/wiki/Estradiol_17-beta-dehydrogenase Estradiol 17-beta-dehydrogenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.62 1.1.1.62]]. Structure known Active Site: CAT. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BHS OCA]].
+
*[[Hydroxysteroid dehydrogenase 3D structures|Hydroxysteroid dehydrogenase 3D structures]]
-
 
+
__TOC__
-
==Reference==
+
</StructureSection>
-
Structure of human estrogenic 17 beta-hydroxysteroid dehydrogenase at 2.20 A resolution., Ghosh D, Pletnev VZ, Zhu DW, Wawrzak Z, Duax WL, Pangborn W, Labrie F, Lin SX, Structure. 1995 May 15;3(5):503-13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7663947 7663947]
+
-
[[Category: Estradiol 17-beta-dehydrogenase]]
+
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Ghosh, D.]]
+
[[Category: Ghosh D]]
-
[[Category: estrogen]]
+
-
[[Category: human placental 17beta-hsd]]
+
-
[[Category: human type i 17beta-hsd]]
+
-
[[Category: oxidoreductase]]
+
-
[[Category: short-chain dehydrogenase]]
+
-
[[Category: steroid dehydrogenase]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 14:54:57 2007''
+

Current revision

HUMAN ESTROGENIC 17BETA-HYDROXYSTEROID DEHYDROGENASE

PDB ID 1bhs

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools