Wild-type rat anionic trypsin complexed with bovine pancreatic trypsin inhibitor (BPTI). Determined by X-ray diffraction at 1.8 Å resolution. Released 23 Dec 1998.
Explore 3TGI in 3D Show helices and sheets RCSB PDB PDBe
3TGI contains 12 α-helices and 24 β-strands across 2 chains. Residue ranges use author residue numbering, as in the PDB file, from PDBe. To see them in 3D, choose the Cartoon representation with Secondary structure coloring: helices, sheets and coils get different colors.
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 17 | 1 | 1 |
| β-strand | 20-21 | 2 | 2 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-34 | 5 | 3 |
| β-strand | 40-48 | 9 | 3 |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 56-58 | 3 | |
| β-strand | 64-68 | 4 | 3 |
| β-strand | 72 | 1 | 4 |
| β-strand | 81-90 | 10 | 3 |
| β-strand | 104-108 | 5 | 3 |
| β-strand | 122 | 1 | 2 |
| α-helix | 123-124 | 2 | |
| α-helix | 128-130 | 3 | |
| β-strand | 135-140 | 6 | 2 |
| β-strand | 154 | 1 | 4 |
| α-helix | 155 | 1 | |
| β-strand | 156-162 | 7 | 2 |
| α-helix | 163-164 | 2 | |
| α-helix | 165-171 | 7 | |
| β-strand | 180-183 | 4 | 2 |
| β-strand | 189 | 1 | 1 |
| β-strand | 198-201 | 4 | 2 |
| β-strand | 204-215 | 8 | 2 |
| β-strand | 221A | 1 | 5 |
| β-strand | 224 | 1 | 5 |
| β-strand | 226-230 | 5 | 2 |
| α-helix | 231-233 | 3 | |
| α-helix | 235-244 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 3-6 | 4 | |
| α-helix | 8-9 | 2 | |
| β-strand | 14 | 1 | 2 |
| β-strand | 18-24 | 7 | 6 |
| β-strand | 29-35 | 7 | 6 |
| β-strand | 45 | 1 | 6 |
| α-helix | 48-55 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Trypsin | E | protein | 223 | Rattus norvegicus | P00763 (AlphaFold model) |
| Bovine pancreatic trypsin inhibitor | I | protein | 65 | Bos taurus | P00974 (AlphaFold model) |
>3TGI_1 TRYPSIN (chains E) IVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRLGEHNINVLEG NEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKLNARVATVALPSSCAPAGTQCLISG WGNTLSSGVNEPDLLQCLDAPLLPQADCEASYPGKITDNMVCVGFLEGGKDSCQGDSGGP VVCNGELQGIVSWGYGCALPDNPGVYTKVCNYVDWIQDTIAAN
>3TGI_2 BOVINE PANCREATIC TRYPSIN INHIBITOR (chains I) RPDFCLEPPYTGPCKARIIRYFYNAKAGLCQTFVYGGCRAKRNNFKSAEDCMRTCGGAIG PWENL
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 1 |
Water and common crystallization additives (SO4) are not listed.
Comparison of Anionic and Cationic Trypsinogens: The Anionic Activation Domain is More Flexible in Solution and Differs in its Mode of Bpti Binding in the Crystal Structure. Pasternak, A., Ringe, D., Hedstrom, L. Protein Sci (1999) 8:253-258. PubMed
Other PDB entries of the same protein (UniProt P00763 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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