1qmu
From Proteopedia
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| - | [[Image:1qmu.jpg|left|200px]] | + | [[Image:1qmu.jpg|left|200px]] |
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| - | '''DUCK CARBOXYPEPTIDASE D DOMAIN II''' | + | {{Structure |
| + | |PDB= 1qmu |SIZE=350|CAPTION= <scene name='initialview01'>1qmu</scene>, resolution 2.70Å | ||
| + | |SITE= <scene name='pdbsite=ZN:Zn+Binding+Site'>ZN</scene> | ||
| + | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''DUCK CARBOXYPEPTIDASE D DOMAIN II''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1QMU is a [ | + | 1QMU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Anas_specularioides Anas specularioides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QMU OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily., Gomis-Ruth FX, Companys V, Qian Y, Fricker LD, Vendrell J, Aviles FX, Coll M, EMBO J. 1999 Nov 1;18(21):5817-26. PMID:[http:// | + | Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily., Gomis-Ruth FX, Companys V, Qian Y, Fricker LD, Vendrell J, Aviles FX, Coll M, EMBO J. 1999 Nov 1;18(21):5817-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10545093 10545093] |
[[Category: Anas specularioides]] | [[Category: Anas specularioides]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zinc-dependent protease]] | [[Category: zinc-dependent protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:39:51 2008'' |
Revision as of 11:39, 20 March 2008
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| , resolution 2.70Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
DUCK CARBOXYPEPTIDASE D DOMAIN II
Overview
The crystal structure of domain II of duck carboxypeptidase D, a prohormone/propeptide processing enzyme integrated in a three repeat tandem in the natural system, has been solved, constituting a prototype for members of the regulatory metallocarboxypeptidase subfamily. It displays a 300 residue N-terminal alpha/beta-hydrolase subdomain with overall topological similarity to and general coincidence of the key catalytic residues with the archetypal pancreatic carboxypeptidase A. However, numerous significant insertions/deletions in segments forming the funnel-like access to the active site explain differences in specificity towards larger protein substrates or inhibitors. This alpha/beta-hydrolase subdomain is followed by a C-terminal 80 residue beta-sandwich subdomain, unique for these regulatory metalloenzymes and topologically related to transthyretin and sugar-binding proteins. The structure described here establishes the fundamentals for a better understanding of the mechanism ruling events such as prohormone processing and will enable modelling of regulatory carboxypeptidases as well as a more rational design of inhibitors of carboxypeptidase D.
About this Structure
1QMU is a Single protein structure of sequence from Anas specularioides. Full crystallographic information is available from OCA.
Reference
Crystal structure of avian carboxypeptidase D domain II: a prototype for the regulatory metallocarboxypeptidase subfamily., Gomis-Ruth FX, Companys V, Qian Y, Fricker LD, Vendrell J, Aviles FX, Coll M, EMBO J. 1999 Nov 1;18(21):5817-26. PMID:10545093
Page seeded by OCA on Thu Mar 20 13:39:51 2008
