Rat trypsinogen K15A complexed with bovine pancreatic trypsin inhibitor. Determined by X-ray diffraction at 1.55 Å resolution. Released 4 Jul 2001.
Explore 1F7Z in 3D Show helices and sheets RCSB PDB PDBe
1F7Z contains 13 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 |
| α-helix | 111-114 | 4 | |
| 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 | 235-243 | 9 |
| 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 II, anionic | A | protein | 233 | Rattus norvegicus | P00763 (AlphaFold model) |
| Pancreatic trypsin inhibitor | I | protein | 65 | Bos taurus | P00974 (AlphaFold model) |
>1F7Z_1 TRYPSIN II, ANIONIC (chains A) EAFPVDDDDAIVGGYTCQENSVPYQVSLNSGYHFCGGSLINDQWVVSAAHCYKSRIQVRL GEHNINVLEGNEQFVNAAKIIKHPNFDRKTLNNDIMLIKLSSPVKLNARVATVALPSSCA PAGTQCLISGWGNTLSSGVNEPDLLQCLDAPLLPQADCEASYPGKITDNMVCVGFLEGGK DSCQGDSGGPVVCNGELQGIVSWGYGCALPDNPGVYTKVCNYVDWIQDTIAAN
>1F7Z_2 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.
The energetic cost of induced fit catalysis: Crystal structures of trypsinogen mutants with enhanced activity and inhibitor affinity. Pasternak, A., White, A., Jeffery, C.J. et al. Protein Sci (2001) 10:1331-1342. DOI 10.1110/ps.44101 · 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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