7xf9
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<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> | <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='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> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.2Å</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). | |
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
Crystal structure of human bleomycin hydrolase H372A mutant
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Categories: Homo sapiens | Large Structures | Chang CY | Huang SJ | Lin EC | Toh SI | Wang YL | Zheng YZ
