TMPRSS2 complexed with the noncovalent inhibitor 6-amidino-2-napthol. Determined by X-ray diffraction at 2.19 Å resolution. Released 7 Feb 2024.
Explore 8V1F in 3D Show helices and sheets RCSB PDB PDBe
8V1F contains 24 α-helices and 60 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 | 149-152 | 4 | 1 |
| β-strand | 157-162 | 6 | 1 |
| β-strand | 167-170 | 4 | 1 |
| β-strand | 171 | 1 | 2 |
| β-strand | 172 | 1 | 1 |
| α-helix | 178-187 | 10 | |
| β-strand | 196-200 | 5 | 1 |
| β-strand | 209-212 | 4 | 2 |
| α-helix | 221-224 | 4 | |
| β-strand | 225-228 | 4 | 2 |
| β-strand | 236-240 | 5 | 1 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 257 | 1 | 3 |
| β-strand | 260-261 | 2 | 4 |
| α-helix | 262-263 | 2 | |
| β-strand | 270-275 | 6 | 5 |
| β-strand | 278-285 | 8 | 5 |
| β-strand | 290-293 | 4 | 5 |
| α-helix | 295-298 | 4 | |
| α-helix | 305-307 | 3 | |
| β-strand | 308-312 | 5 | 5 |
| β-strand | 316 | 1 | 6 |
| α-helix | 317-319 | 3 | |
| β-strand | 326-333 | 8 | 5 |
| β-strand | 338 | 1 | 7 |
| β-strand | 343 | 1 | 7 |
| β-strand | 347-351 | 5 | 5 |
| α-helix | 363-364 | 2 | |
| β-strand | 365 | 1 | 4 |
| α-helix | 366-368 | 3 | |
| β-strand | 378-383 | 6 | 4 |
| α-helix | 392-394 | 3 | |
| β-strand | 396 | 1 | 6 |
| β-strand | 398-405 | 8 | 4 |
| α-helix | 407-410 | 4 | |
| β-strand | 424-428 | 5 | 4 |
| β-strand | 435 | 1 | 3 |
| β-strand | 444-449 | 6 | 4 |
| β-strand | 452-461 | 10 | 4 |
| β-strand | 472-476 | 5 | 4 |
| α-helix | 477-480 | 4 | |
| α-helix | 481-490 | 10 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 257 | 1 | 10 |
| β-strand | 260-261 | 2 | 11 |
| α-helix | 262-263 | 2 | |
| β-strand | 270-275 | 6 | 12 |
| β-strand | 278-285 | 8 | 12 |
| β-strand | 290-293 | 4 | 12 |
| α-helix | 295-298 | 4 | |
| α-helix | 305-307 | 3 | |
| β-strand | 308-312 | 5 | 12 |
| β-strand | 316 | 1 | 13 |
| α-helix | 317-319 | 3 | |
| β-strand | 322 | 1 | 14 |
| β-strand | 324 | 1 | 14 |
| β-strand | 326-333 | 8 | 12 |
| β-strand | 338 | 1 | 15 |
| β-strand | 343 | 1 | 15 |
| β-strand | 347-351 | 5 | 12 |
| α-helix | 354-357 | 4 | |
| α-helix | 363-364 | 2 | |
| β-strand | 365 | 1 | 11 |
| α-helix | 366-368 | 3 | |
| β-strand | 378-383 | 6 | 11 |
| β-strand | 396 | 1 | 13 |
| β-strand | 398-405 | 8 | 11 |
| α-helix | 407-410 | 4 | |
| β-strand | 424-428 | 5 | 11 |
| β-strand | 435 | 1 | 10 |
| β-strand | 444-449 | 6 | 11 |
| β-strand | 452-461 | 10 | 11 |
| β-strand | 472-476 | 5 | 11 |
| α-helix | 477-480 | 4 | |
| α-helix | 481-491 | 11 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Transmembrane protease serine 2 non-catalytic chain | A, C | protein | 110 | Homo sapiens | O15393 (AlphaFold model) |
| Transmembrane protease serine 2 | B, D | protein | 249 | Homo sapiens | O15393 (AlphaFold model) |
>8V1F_1 Transmembrane protease serine 2 non-catalytic chain (chains A, C) AACVRLYGPNFILQVYSSQRKSWHPVCQDDWNENYGRAACRDMGYKNNFYSSQGIVDDSG STSFMKLNTSAGNVDIYKKLYHSDACSSKAVVSLRCIACGVNLNSDDDDK
>8V1F_2 Transmembrane protease serine 2 (chains B, D) IVGGESALPGAWPWQVSLHVQNVHVCGGSIITPEWIVTAAHCVEKPLNNPWHWTAFAGIL RQSFMFYGAGYQVEKVISHPNYDSKTKNNDIALMKLQKPLTFNDLVKPVCLPNPGMMLQP EQLCWISGWGATEEKGKTSEVLNAAKVLLIETQRCNSRYVYDNLITPAMICAGFLQGNVD SCQGDSGGPLVTSKNNIWWLIGDTSWGSGCAKAYRPGVYGNVMVFTDWIYRQMRADGEFV EHHHHHHHH
| ID | Name | Formula | Copies |
|---|---|---|---|
| TAM | Tris(hydroxyethyl)aminomethane | C7 H17 N O3 | 4 |
| 7R8 | 6-oxidanylnaphthalene-2-carboximidamide | C11 H10 N2 O | 2 |
| CIT | Citric acid | C6 H8 O7 | 2 |
Water and common crystallization additives (UNX, EDO, PEG, PG4) are not listed.
Large Library Docking and Biophysical Analysis of Small-Molecule TMPRSS2 Inhibitors. Fraser, B.J., Young, N.J., Bender, B.J. et al. J Med Chem (2025) 68:19893-19907. DOI 10.1021/acs.jmedchem.4c03089 · PubMed
Other PDB entries of the same protein (UniProt O15393 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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