Human beta-tryptase co-crystal structure with (6S,8R)-N,N'-bis[3-({4-[3-(aminomethyl)phenyl]piperidin-1-yl}carbonyl)phenyl]-8-hydroxy-6-(1-hydroxycyclobutyl)-5,7-dioxaspiro[3.4]octane-6,8-dicarboxamide. Determined by X-ray diffraction at 1.65 Å resolution. Released 18 Mar 2015.
Explore 4MPU in 3D Show helices and sheets RCSB PDB PDBe
4MPU contains 19 α-helices and 51 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 | 32 | 1 | 1 |
| β-strand | 35-36 | 2 | 2 |
| α-helix | 37-38 | 2 | |
| β-strand | 45-50 | 6 | 3 |
| β-strand | 56-65 | 10 | 3 |
| β-strand | 68-71 | 4 | 3 |
| α-helix | 73-76 | 4 | |
| β-strand | 79 | 1 | 4 |
| α-helix | 83-85 | 3 | |
| β-strand | 86-89 | 4 | 3 |
| β-strand | 94 | 1 | 5 |
| β-strand | 102-109 | 8 | 3 |
| β-strand | 123-127 | 5 | 3 |
| α-helix | 130-133 | 4 | |
| β-strand | 134 | 1 | 6 |
| β-strand | 137 | 1 | 6 |
| α-helix | 139-140 | 2 | |
| β-strand | 141 | 1 | 2 |
| α-helix | 142-144 | 3 | |
| β-strand | 155-159 | 5 | 2 |
| β-strand | 164 | 1 | 7 |
| β-strand | 167 | 1 | 7 |
| α-helix | 168-170 | 3 | |
| β-strand | 174 | 1 | 5 |
| β-strand | 176-179 | 4 | 2 |
| β-strand | 182-183 | 2 | 2 |
| α-helix | 185-193 | 9 | |
| β-strand | 196 | 1 | 8 |
| β-strand | 209-212 | 4 | 2 |
| β-strand | 218 | 1 | 1 |
| β-strand | 227-232 | 6 | 2 |
| β-strand | 235-244 | 10 | 2 |
| β-strand | 250 | 1 | 9 |
| β-strand | 253 | 1 | 9 |
| β-strand | 255-259 | 5 | 2 |
| α-helix | 260-263 | 4 | |
| α-helix | 264-268 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 32 | 1 | 10 |
| β-strand | 35-36 | 2 | 11 |
| α-helix | 37-38 | 2 | |
| β-strand | 45-50 | 6 | 12 |
| β-strand | 56-65 | 10 | 12 |
| β-strand | 68-71 | 4 | 12 |
| α-helix | 73-76 | 4 | |
| β-strand | 79 | 1 | 8 |
| α-helix | 83-85 | 3 | |
| β-strand | 86-89 | 4 | 12 |
| β-strand | 94 | 1 | 13 |
| β-strand | 102-109 | 8 | 12 |
| β-strand | 123-127 | 5 | 12 |
| α-helix | 139-140 | 2 | |
| β-strand | 141 | 1 | 11 |
| α-helix | 142-144 | 3 | |
| β-strand | 154-159 | 6 | 11 |
| β-strand | 164 | 1 | 14 |
| β-strand | 167 | 1 | 14 |
| α-helix | 168-170 | 3 | |
| β-strand | 174 | 1 | 13 |
| β-strand | 176-183 | 8 | 11 |
| α-helix | 185-193 | 9 | |
| β-strand | 196 | 1 | 4 |
| β-strand | 209-212 | 4 | 11 |
| β-strand | 218 | 1 | 10 |
| β-strand | 227-232 | 6 | 11 |
| β-strand | 235-244 | 10 | 11 |
| β-strand | 250 | 1 | 15 |
| β-strand | 253 | 1 | 15 |
| β-strand | 255-259 | 5 | 11 |
| α-helix | 261-263 | 3 | |
| α-helix | 264-268 | 5 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Tryptase alpha/beta-1 | A, B | protein | 245 | Homo sapiens | Q15661 (AlphaFold model) |
>4MPU_1 Tryptase alpha/beta-1 (chains A, B) IVGGQEAPRSKWPWQVSLRVHGPYWMHFCGGSLIHPQWVLTAAHCVGPDVKDLAALRVQL REQHLYYQDQLLPVSRIIVHPQFYTAQIGADIALLELEEPVKVSSHVHTVTLPPASETFP PGMPCWVTGWGDVDNDERLPPPFPLKQVKVPIMENHICDAKYHLGAYTGDDVRIVRDDML CAGNTRRDSCQGDSGGPLVCKVNGTWLQAGVVSWGEGCAQPNRPGIYTRVTYYLDWIHHY VPKKP
| ID | Name | Formula | Copies |
|---|---|---|---|
| X2A | (6S,8R)-N,N'-bis[3-({4-[3-(aminomethyl)phenyl]piperidin-1-yl}carbonyl)phenyl]-8… | C50 H58 N6 O8 | 1 |
Water and common crystallization additives (MES, SO4, PG4) are not listed.
Target-Directed Self-Assembly of Homodimeric Drugs Against beta-Tryptase. Giardina, S.F., Werner, D.S., Pingle, M. et al. ACS Med Chem Lett (2018) 9:827-831. DOI 10.1021/acsmedchemlett.8b00204 · PubMed
Other PDB entries of the same protein (UniProt Q15661 (AlphaFold model), which also has an AlphaFold model), best resolution first:
MolViewer shows 4MPU directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.