Mesotrypsin in complex with cleaved amyloid precursor like protein 2 inhibitor (APLP2). Determined by X-ray diffraction at 1.4 Å resolution. Released 9 Nov 2016.
Explore 5JBT in 3D Show helices and sheets RCSB PDB PDBe
5JBT contains 11 α-helices and 25 β-strands across 3 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 | 64-67 | 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 | 115 | 1 | 5 |
| β-strand | 118 | 1 | 5 |
| β-strand | 122 | 1 | 2 |
| α-helix | 123-124 | 2 | |
| β-strand | 135-140 | 6 | 2 |
| β-strand | 154 | 1 | 4 |
| 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 | 226-230 | 5 | 2 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-244 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 5 | 1 | 6 |
| α-helix | 9-10 | 2 | |
| β-strand | 14 | 1 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 20-24 | 5 | 6 |
| β-strand | 29-33 | 5 | 6 |
| α-helix | 40-42 | 3 | |
| β-strand | 46 | 1 | 6 |
| α-helix | 48-54 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| PRSS3 protein | A | protein | 224 | Homo sapiens | P35030 (AlphaFold model) |
| Amyloid-like protein 2 | X | protein | 14 | Homo sapiens | Q06481 (AlphaFold model) |
| Amyloid-like protein 2 | Y | protein | 38 | Homo sapiens | Q06481 (AlphaFold model) |
>5JBT_1 PRSS3 protein (chains A) IVGGYTCEENSLPYQVSLNSGSHFCGGSLISEQWVVSAAHCYKTRIQVRLGEHNIKVLEG NEQFINAAKIIRHPKYNRDTLDNDIMLIKLSSPAVINARVSTISLPTAPPAAGTECLISG WGNTLSFGADYPDELKCLDAPVLTQAECKASYPGKITNSMFCVGFLEGGKDSCQRDAGGP VVCNGQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDTIAANS
>5JBT_2 Amyloid-like protein 2 (chains X) KAVCSQEAMTGPCR
>5JBT_3 Amyloid-like protein 2 (chains Y) MPRWYFDLSKGKCVRFIYGGCGGNRNNFESEDYCMAVC
| ID | Name | Formula | Copies |
|---|---|---|---|
| CA | Calcium ion | Ca | 1 |
Water and common crystallization additives (SO4) are not listed.
An Acrobatic Substrate Metamorphosis Reveals a Requirement for Substrate Conformational Dynamics in Trypsin Proteolysis. Kayode, O., Wang, R., Pendlebury, D.F. et al. J Biol Chem (2016) 291:26304-26319. DOI 10.1074/jbc.M116.758417 · PubMed
Other PDB entries of the same protein (UniProt P35030 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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