5ZEQ
Carboxypeptidase B in complex with DD28
Summary for 5ZEQ
| Entry DOI | 10.2210/pdb5zeq/pdb |
| Descriptor | Carboxypeptidase B, ZINC ION, (2~{S})-2-[(6-azanyl-5-chloranyl-pyridin-3-yl)methyl]-3-selanyl-propanoic acid, ... (5 entities in total) |
| Functional Keywords | selenium, organoselenium, selenol, cpb inhibitor, selectivity, hydrolase-inhibitor complex, hydrolase/inhibitor |
| Biological source | Sus scrofa (Pig) |
| Total number of polymer chains | 1 |
| Total formula weight | 35426.12 |
| Authors | Itoh, T.,Yoshimoto, N.,Yamamoto, K. (deposition date: 2018-02-27, release date: 2018-06-20, Last modification date: 2024-10-09) |
| Primary citation | Itoh, T.,Yoshimoto, N.,Hirano, Y.,Yamamoto, K. Structural basis for the selective inhibition of activated thrombin-activatable fibrinolysis inhibitor (TAFIa) by a selenium-containing inhibitor with chloro-aminopyridine as a basic group Bioorg. Med. Chem. Lett., 28:2256-2260, 2018 Cited by PubMed Abstract: Activated thrombin-activatable fibrinolysis inhibitor (TAFIa) is a target molecule for treating thromboembolic disorders. We previously reported that design and synthesis of compound 1 containing a selenol group and chloloaminopyridine. Compound 1 showed high inhibitory activity towards TAFIa, with a high degree of selectivity for TAFIa over carboxypeptidase N (CPN). Here we report investigation of this selectivity. To obtain co-crystal of 1/pp-CPB (a surrogate of TAFIa), we synthesized protected compound 5 as a stabilized precursor of 1. The X-ray crystal structure and docking study indicated that the Cl substituent is accommodated in the pp-CPB specific pocket whereas CPN has no identical pocket. This is important information for the design of drugs targeting TAFIa with high selectivity. PubMed: 29859906DOI: 10.1016/j.bmcl.2018.05.042 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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