Trypsin inhibitor from soybean (STI). Determined by X-ray diffraction at 2.3 Å resolution. Released 28 Oct 1998.
Explore 1AVU in 3D Show helices and sheets RCSB PDB PDBe
1AVU contains 3 α-helices and 20 β-strands across 1 chain. 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 | 2 | 1 | 1 |
| β-strand | 4-5 | 2 | 2 |
| β-strand | 9-10 | 2 | 2 |
| α-helix | 11 | 1 | |
| β-strand | 12 | 1 | 3 |
| β-strand | 15-21 | 7 | 4 |
| β-strand | 29-32 | 4 | 4 |
| β-strand | 42-45 | 4 | 4 |
| β-strand | 56-59 | 4 | 4 |
| β-strand | 66 | 1 | 3 |
| β-strand | 68 | 1 | 1 |
| β-strand | 73-77 | 5 | 4 |
| α-helix | 84-86 | 3 | |
| β-strand | 92 | 1 | 4 |
| β-strand | 94-96 | 3 | 4 |
| β-strand | 104-106 | 3 | 4 |
| β-strand | 113-114 | 2 | 4 |
| β-strand | 116-122 | 7 | 4 |
| β-strand | 131-137 | 7 | 4 |
| β-strand | 146-152 | 7 | 4 |
| β-strand | 159-164 | 6 | 4 |
| α-helix | 168-170 | 3 | |
| β-strand | 171-175 | 5 | 4 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Trypsin inhibitor | A | protein | 181 | Glycine max | P01070 (AlphaFold model) |
>1AVU_1 TRYPSIN INHIBITOR (chains A) DFVLDNEGNPLENGGTYYILSDITAFGGIRAAPTGNERCPLTVVQSRNELDKGIGTIISS PYRIRFIAEGHPLSLKFDSFAVIMLCVGIPTEWSVVEDLPEGPAVKIGENKDAMDGWFRL ERVSDDEFNNYKLVFCPQQAEDDKCGDIGISIDHDDGTRRLVVSKNKPLVVQFQKLDKES L
Kunitz-type soybean trypsin inhibitor revisited: refined structure of its complex with porcine trypsin reveals an insight into the interaction between a homologous inhibitor from Erythrina caffra and tissue-type plasminogen activator. Song, H.K., Suh, S.W. J Mol Biol (1998) 275:347-363. DOI 10.1006/jmbi.1997.1469 · PubMed
Other PDB entries of the same protein (UniProt P01070 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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