1.2A resolution structure of a crayfish trypsin complexed with a peptide inhibitor, SGTI. Determined by X-ray diffraction at 1.2 Å resolution. Released 18 Apr 2006.
Explore 2F91 in 3D Show helices and sheets RCSB PDB PDBe
2F91 contains 6 α-helices and 23 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 |
| β-strand | 30-37 | 8 | 3 |
| β-strand | 37C-48 | 12 | 3 |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 56-58 | 3 | |
| β-strand | 64-68 | 5 | 3 |
| β-strand | 72 | 1 | 4 |
| β-strand | 81-90 | 10 | 3 |
| β-strand | 104-108 | 5 | 3 |
| β-strand | 115 | 1 | 5 |
| β-strand | 118 | 1 | 5 |
| α-helix | 120-121 | 2 | |
| β-strand | 122 | 1 | 2 |
| α-helix | 123-125 | 3 | |
| β-strand | 135-140 | 6 | 2 |
| β-strand | 154 | 1 | 4 |
| β-strand | 156-163 | 8 | 2 |
| α-helix | 165-172 | 8 | |
| β-strand | 180-183 | 4 | 2 |
| β-strand | 189 | 1 | 1 |
| β-strand | 198-201 | 4 | 2 |
| β-strand | 208-216 | 9 | 2 |
| β-strand | 227-231 | 5 | 2 |
| α-helix | 232-234 | 3 | |
| α-helix | 236-242 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 9-12 | 4 | 2 |
| β-strand | 15-19 | 5 | 2 |
| β-strand | 25-28 | 4 | 2 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| hepatopancreas trypsin | A | protein | 237 | Pontastacus leptodactylus | Q52V24 (AlphaFold model) |
| Serine protease inhibitor I/II | B | protein | 35 | O46162 (AlphaFold model) |
>2F91_1 hepatopancreas trypsin (chains A) IVGGTDATLGEFPYQLSFQETFIGFSFHFCGASIYNENYAITAGHCVYGDDYENPSGLQI VAGELDMSVNEGSEQIITVSKIILHENFDYNLLDNDISLLKLSGSLTFNDNVAPIALPEQ GHTATGDVIVTGWGTTSEGGNTPDVLQKVTVPLVSDEDCRADYGADEILDSMICAGVPEG GKDSCQGDSGGPLAASDTGSTYLAGIVSWGYGCARPGYPGVYTEVSYHVDWIKANAV
>2F91_2 Serine protease inhibitor I/II (chains B) EQECTPGQTKKQDCNTCNCTPTGVWACTRKGCPPH
| ID | Name | Formula | Copies |
|---|---|---|---|
| CD | Cadmium ion | Cd | 6 |
Water and common crystallization additives (CL) are not listed.
Enzyme:Substrate Hydrogen Bond Shortening during the Acylation Phase of Serine Protease Catalysis. Fodor, K., Harmat, V., Neutze, R. et al. Biochemistry (2006) 45:2114-2121. DOI 10.1021/bi0517133 · PubMed
Other PDB entries of the same protein (UniProt Q52V24 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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