1ATB
HIGH-RESOLUTION STRUCTURE OF ASCARIS TRYPSIN INHIBITOR IN SOLUTION: DIRECT EVIDENCE FOR A PH INDUCED CONFORMATIONAL TRANSITION IN THE REACTIVE SITE
Summary for 1ATB
| Entry DOI | 10.2210/pdb1atb/pdb |
| Descriptor | ASCARIS TRYPSIN INHIBITOR (1 entity in total) |
| Functional Keywords | proteinase inhibitor(trypsin) |
| Biological source | Ascaris suum (pig roundworm) |
| Total number of polymer chains | 1 |
| Total formula weight | 6807.85 |
| Authors | Clore, G.M.,Grasberger, B.L.,Gronenborn, A.M. (deposition date: 1994-05-20, release date: 1994-08-31, Last modification date: 2024-11-20) |
| Primary citation | Grasberger, B.L.,Clore, G.M.,Gronenborn, A.M. High-resolution structure of Ascaris trypsin inhibitor in solution: direct evidence for a pH-induced conformational transition in the reactive site. Structure, 2:669-678, 1994 Cited by PubMed Abstract: The Ascaris trypsin inhibitor (ATI) is a member of a new family of serine protease inhibitors isolated from the helminthic worm Ascaris lumbricoides var suum. This family comprises five chymotrypsin/elastase inhibitors and one trypsin inhibitor. Members are characterized by the presence of five disulfide bonds (two of which are located on either side of the reactive site) in a single small protein domain of 61-62 residues. PubMed: 7922043DOI: 10.1016/S0969-2126(00)00067-8 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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