1htd

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|PDB= 1htd |SIZE=350|CAPTION= <scene name='initialview01'>1htd</scene>, resolution 2.1&Aring;
|PDB= 1htd |SIZE=350|CAPTION= <scene name='initialview01'>1htd</scene>, resolution 2.1&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Atrolysin_C Atrolysin C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.42 3.4.24.42]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Atrolysin_C Atrolysin C], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.24.42 3.4.24.42] </span>
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1htd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1htd OCA], [http://www.ebi.ac.uk/pdbsum/1htd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1htd RCSB]</span>
}}
}}
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[[Category: Njoroge, F G.]]
[[Category: Njoroge, F G.]]
[[Category: Zhang, D.]]
[[Category: Zhang, D.]]
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[[Category: CA]]
 
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[[Category: ZN]]
 
[[Category: metalloprotease]]
[[Category: metalloprotease]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:41:18 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:10:10 2008''

Revision as of 18:10, 30 March 2008


PDB ID 1htd

Drag the structure with the mouse to rotate
, resolution 2.1Å
Ligands: ,
Activity: Atrolysin C, with EC number 3.4.24.42
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



STRUCTURAL INTERACTION OF NATURAL AND SYNTHETIC INHIBITORS WITH THE VENOM METALLOPROTEINASE, ATROLYSIN C (HT-D)


Overview

The structure of the metalloproteinase and hemorrhagic toxin atrolysin C form d (EC 3.4.24.42), from the venom of the western diamondback rattlesnake Crotalus atrox, has been determined to atomic resolution by x-ray crystallographic methods. This study illuminates the nature of inhibitor binding with natural (< Glu-Asn-Trp, where < Glu is pyroglutamic acid) and synthetic (SCH 47890) ligands. The primary specificity pocket is exceptionally deep; the nature of inhibitor and productive substrate binding is discussed. Insights gained from the study of these complexes facilitate the design of potential drugs to treat diseases where matrix metalloproteinases have been implicated, e.g., arthritis and tumor metastasis.

About this Structure

1HTD is a Single protein structure of sequence from Crotalus atrox. Full crystallographic information is available from OCA.

Reference

Structural interaction of natural and synthetic inhibitors with the venom metalloproteinase, atrolysin C (form d)., Zhang D, Botos I, Gomis-Ruth FX, Doll R, Blood C, Njoroge FG, Fox JW, Bode W, Meyer EF, Proc Natl Acad Sci U S A. 1994 Aug 30;91(18):8447-51. PMID:8078901

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