1TX7
Bovine Trypsin complexed with p-amidinophenylmethylphosphinic acid (AMPA)
Summary for 1TX7
| Entry DOI | 10.2210/pdb1tx7/pdb |
| Descriptor | Trypsinogen, CALCIUM ION, (4-CARBAMIMIDOYLPHENYL)-METHYL-PHOSPHINIC ACID, ... (4 entities in total) |
| Functional Keywords | trypsin, bovine, p-amidinophenylmethylphosphinic acid (ampa), hydrolase |
| Biological source | Bos taurus (cattle) |
| Cellular location | Secreted, extracellular space: P00760 |
| Total number of polymer chains | 1 |
| Total formula weight | 23562.52 |
| Authors | Cui, J.,Marankan, F.,Fu, W.,Crich, D.,Mesecar, A.,Johnson, M.E. (deposition date: 2004-07-02, release date: 2005-09-20, Last modification date: 2024-11-13) |
| Primary citation | Cui, J.,Marankan, F.,Fu, W.,Crich, D.,Mesecar, A.,Johnson, M.E. An oxyanion-hole selective serine protease inhibitor in complex with trypsin. Bioorg.Med.Chem., 10:41-46, 2002 Cited by PubMed Abstract: p-amidinophenylmethylphosphinic acid (AMPA) was designed, synthesized and crystallized in complex with trypsin to study interactions with the oxyanion hole at the S1 site. In comparison to benzamidine, AMPA shows improved activity, which the crystal structure demonstrates to result from hydrogen bonds between the negatively charged phosphinic acid group and the catalytic residues at the oxyanion hole. PubMed: 11738605DOI: 10.1016/S0968-0896(01)00259-0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.75 Å) |
Structure validation
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