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.


7xf9

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 3: Line 3:
<StructureSection load='7xf9' size='340' side='right'caption='[[7xf9]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
<StructureSection load='7xf9' size='340' side='right'caption='[[7xf9]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
-
<table><tr><td colspan='2'>[[7xf9]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7XF9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XF9 FirstGlance]. <br>
+
<table><tr><td colspan='2'>[[7xf9]] 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=7XF9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7XF9 FirstGlance]. <br>
-
</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Bleomycin_hydrolase Bleomycin hydrolase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.40 3.4.22.40] </span></td></tr>
+
</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=7xf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xf9 OCA], [https://pdbe.org/7xf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xf9 RCSB], [https://www.ebi.ac.uk/pdbsum/7xf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xf9 ProSAT]</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=7xf9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7xf9 OCA], [https://pdbe.org/7xf9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7xf9 RCSB], [https://www.ebi.ac.uk/pdbsum/7xf9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7xf9 ProSAT]</span></td></tr>
+
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/BLMH_HUMAN BLMH_HUMAN]] The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B-aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity (By similarity).
+
[[https://www.uniprot.org/uniprot/BLMH_HUMAN BLMH_HUMAN]] The normal physiological role of BLM hydrolase is unknown, but it catalyzes the inactivation of the antitumor drug BLM (a glycopeptide) by hydrolyzing the carboxamide bond of its B-aminoalaninamide moiety thus protecting normal and malignant cells from BLM toxicity (By similarity).
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
Human bleomycin hydrolase (hBH) catalyzes deamidation of the anticancer drug bleomycins (BLM). This enzyme is involved in BLM detoxification and drug resistance. Herein, we report the putative BLM-binding site and catalytic mechanism of hBH. The crystal structures and biochemical studies suggest that hBH cleaves its C-terminal residue without significant preference for the type of amino acid, and therefore can accordingly accommodate the beta-aminoalanine amide moiety of BLM for deamidation. Interestingly, hBH is capable of switching from a cysteine protease to a serine protease that is unable to cleave the secondary amide of hBH C-terminus but reacts with the primary amide of BLMs.
+
-
 
+
-
The Structure-Function Relationship of Human Bleomycin Hydrolase: Mutation of a Cysteine Protease into a Serine Protease.,Zheng YZ, Cui J, Wang YL, Huang SJ, Lin EC, Huang SC, Rudolf JD, Yan X, Chang CY Chembiochem. 2022 Jun 20;23(12):e202200186. doi: 10.1002/cbic.202200186. Epub, 2022 May 5. PMID:35467071<ref>PMID:35467071</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 7xf9" style="background-color:#fffaf0;"></div>
+
-
== References ==
+
-
<references/>
+
__TOC__
__TOC__
</StructureSection>
</StructureSection>
-
[[Category: Bleomycin hydrolase]]
+
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
-
[[Category: Chang, C Y]]
+
[[Category: Chang CY]]
-
[[Category: Huang, S J]]
+
[[Category: Huang SJ]]
-
[[Category: Lin, E C]]
+
[[Category: Lin EC]]
-
[[Category: Toh, S I]]
+
[[Category: Toh SI]]
-
[[Category: Wang, Y L]]
+
[[Category: Wang YL]]
-
[[Category: Zheng, Y Z]]
+
[[Category: Zheng YZ]]
-
[[Category: Cysteine protease]]
+
-
[[Category: Hydrolase]]
+

Revision as of 07:25, 8 September 2022

Crystal structure of human bleomycin hydrolase H372A mutant

PDB ID 7xf9

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7xf9"
Personal tools