1AMH
UNCOMPLEXED RAT TRYPSIN MUTANT WITH ASP 189 REPLACED WITH SER (D189S)
Summary for 1AMH
| Entry DOI | 10.2210/pdb1amh/pdb |
| Descriptor | ANIONIC TRYPSIN, CALCIUM ION (3 entities in total) |
| Functional Keywords | serine protease, activation domain, substrate specificity hydrolase, hydrolase |
| Biological source | Rattus rattus (black rat) |
| Cellular location | Secreted, extracellular space: P00763 |
| Total number of polymer chains | 2 |
| Total formula weight | 47653.81 |
| Authors | Szabo, E.,Bocskei, Z.S.,Naray-Szabo, G.,Graf, L. (deposition date: 1997-06-17, release date: 1997-12-24, Last modification date: 2023-08-02) |
| Primary citation | Szabo, E.,Bocskei, Z.,Naray-Szabo, G.,Graf, L. The three-dimensional structure of Asp189Ser trypsin provides evidence for an inherent structural plasticity of the protease. Eur.J.Biochem., 263:20-26, 1999 Cited by PubMed: 10429182DOI: 10.1046/j.1432-1327.1999.00452.x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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