1QMU
Duck carboxypeptidase D domain II
Summary for 1QMU
| Entry DOI | 10.2210/pdb1qmu/pdb |
| Descriptor | CARBOXYPEPTIDASE GP180 RESIDUES 503-882, alpha-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| Functional Keywords | carboxypeptidase, hydrolase, zinc-dependent protease |
| Biological source | LOPHONETTA SPECULARIOIDES (CRESTED DUCK) |
| Total number of polymer chains | 1 |
| Total formula weight | 45288.38 |
| Authors | Gomis-Rueth, F.X.,Coll, M.,Aviles, F.X.,Vendrell, J.,Fricker, L.D. (deposition date: 1999-10-06, release date: 2000-10-13, Last modification date: 2024-10-23) |
| Primary citation | Gomis-Rueth, F.X.,Companys, V.,Qian, Y.,Fricker, L.D.,Vendrell, J.,Aviles, F.X.,Coll, M. Crystal Structure of Avian Carboxypeptidase D Domain II : A Prototype for the Regulatory Metallocarboxypeptidase Subfamily Embo J., 18:5817-, 1999 Cited by PubMed Abstract: 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. PubMed: 10545093DOI: 10.1093/EMBOJ/18.21.5817 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
Download full validation report
