Human Mesotrypsin in complex with amyloid precursor protein inhibitor variant APPI-M17G/I18F/F34V. Determined by X-ray diffraction at 1.83 Å resolution. Released 4 May 2016.
Explore 5C67 in 3D Show helices and sheets RCSB PDB PDBe
5C67 contains 21 α-helices and 43 β-strands across 4 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 | 30-37 | 6 | 3 |
| β-strand | 39-48 | 10 | 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 | 122 | 1 | 2 |
| α-helix | 123-124 | 2 | |
| α-helix | 128-130 | 3 | |
| 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 | 17 | 1 | 6 |
| β-strand | 20-21 | 2 | 7 |
| α-helix | 22-23 | 2 | |
| β-strand | 30-34 | 5 | 8 |
| β-strand | 40-48 | 9 | 8 |
| β-strand | 51-54 | 4 | 8 |
| α-helix | 56-58 | 3 | |
| β-strand | 64-67 | 4 | 8 |
| β-strand | 72 | 1 | 9 |
| β-strand | 81-90 | 10 | 8 |
| β-strand | 104-108 | 5 | 8 |
| α-helix | 122-124 | 3 | |
| β-strand | 135-140 | 6 | 7 |
| β-strand | 154 | 1 | 9 |
| β-strand | 156-162 | 7 | 7 |
| α-helix | 163-164 | 2 | |
| α-helix | 165-171 | 7 | |
| β-strand | 180-183 | 4 | 7 |
| β-strand | 189 | 1 | 6 |
| β-strand | 198-201 | 4 | 7 |
| β-strand | 204-215 | 8 | 7 |
| β-strand | 226-230 | 5 | 7 |
| α-helix | 231-234 | 4 | |
| α-helix | 235-244 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 8-9 | 2 | |
| β-strand | 14 | 1 | 7 |
| β-strand | 18-24 | 7 | 10 |
| β-strand | 29-35 | 7 | 10 |
| β-strand | 45 | 1 | 10 |
| α-helix | 48-54 | 7 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 4-6 | 3 | |
| α-helix | 8-9 | 2 | |
| β-strand | 14 | 1 | 2 |
| β-strand | 18-24 | 7 | 5 |
| β-strand | 29-35 | 7 | 5 |
| β-strand | 45 | 1 | 5 |
| α-helix | 48-55 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Trypsin-3 | A, B | protein | 224 | Homo sapiens | P35030 (AlphaFold model) |
| Amyloid beta A4 protein | C, E | protein | 81 | Homo sapiens | P05067 (AlphaFold model) |
>5C67_1 Trypsin-3 (chains A, B) IVGGYTCEENSLPYQVSLNSGSHFCGGSLISEQWVVSAAHCYKTRIQVRLGEHNIKVLEG NEQFINAAKIIRHPKYNRDTLDNDIMLIKLSSPAVINARVSTISLPTAPPAAGTECLISG WGNTLSFGADYPDELKCLDAPVLTQAECKASYPGKITNSMFCVGFLEGGKDSCQRDAGGP VVCNGQLQGVVSWGHGCAWKNRPGVYTKVYNYVDWIKDTIAANS
>5C67_2 Amyloid beta A4 protein (chains C, E) YVDYKDDDDKEFEVCSEQAETGPCRAGFSRWYFDVTEGKCAPFVYGGCGGNRNNFDTEEY CMAVCGSAIPRHHHHHHAAAN
Combinatorial protein engineering of proteolytically resistant mesotrypsin inhibitors as candidates for cancer therapy. Cohen, I., Kayode, O., Hockla, A. et al. Biochem J (2016) 473:1329-1341. DOI 10.1042/BJ20151410 · 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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