1qmu
From Proteopedia
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|PDB= 1qmu |SIZE=350|CAPTION= <scene name='initialview01'>1qmu</scene>, resolution 2.70Å | |PDB= 1qmu |SIZE=350|CAPTION= <scene name='initialview01'>1qmu</scene>, resolution 2.70Å | ||
|SITE= <scene name='pdbsite=ZN:Zn+Binding+Site'>ZN</scene> | |SITE= <scene name='pdbsite=ZN:Zn+Binding+Site'>ZN</scene> | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1qmu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qmu OCA], [http://www.ebi.ac.uk/pdbsum/1qmu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qmu RCSB]</span> | ||
}} | }} | ||
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[[Category: Gomis-Rueth, F X.]] | [[Category: Gomis-Rueth, F X.]] | ||
[[Category: Vendrell, J.]] | [[Category: Vendrell, J.]] | ||
| - | [[Category: SO4]] | ||
| - | [[Category: ZN]] | ||
[[Category: carboxypeptidase]] | [[Category: carboxypeptidase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: zinc-dependent protease]] | [[Category: zinc-dependent protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:16:02 2008'' |
Revision as of 20:16, 30 March 2008
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| , resolution 2.70Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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 Sun Mar 30 23:16:02 2008
