Crystal structure of uPA in complex with upain-2-2. Determined by X-ray diffraction at 1.46 Å resolution. Released 11 Jul 2018.
Explore 5WXF in 3D Show helices and sheets RCSB PDB PDBe
5WXF contains 11 α-helices and 22 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 | 17 | 1 | 1 |
| β-strand | 20-21 | 2 | 2 |
| α-helix | 24-26 | 3 | |
| β-strand | 30-36 | 7 | 3 |
| α-helix | 37 | 1 | |
| β-strand | 38-48 | 11 | 3 |
| β-strand | 51-54 | 4 | 3 |
| α-helix | 56-58 | 3 | |
| α-helix | 62-63 | 3 | |
| β-strand | 64-68 | 5 | 3 |
| β-strand | 72 | 1 | 4 |
| β-strand | 81-90 | 10 | 3 |
| β-strand | 95 | 1 | 5 |
| β-strand | 100 | 1 | 5 |
| β-strand | 104-109 | 6 | 3 |
| β-strand | 122 | 1 | 2 |
| α-helix | 123-125 | 3 | |
| α-helix | 130-131 | 2 | |
| β-strand | 135-140 | 6 | 2 |
| α-helix | 151-152 | 2 | |
| β-strand | 154 | 1 | 4 |
| β-strand | 156-163 | 8 | 2 |
| α-helix | 165-169 | 5 | |
| α-helix | 173-175 | 3 | |
| β-strand | 180-184 | 5 | 2 |
| β-strand | 189 | 1 | 1 |
| β-strand | 198-203 | 6 | 2 |
| β-strand | 206-215 | 10 | 2 |
| β-strand | 222 | 1 | 6 |
| β-strand | 224 | 1 | 6 |
| β-strand | 226-230 | 5 | 2 |
| α-helix | 231-233 | 3 | |
| α-helix | 235-242 | 8 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Urokinase-type plasminogen activator chain B | U | protein | 253 | Homo sapiens | P00749 (AlphaFold model) |
| upain-2-2 peptide | P | protein | 12 | Phage display vector pTDisp |
>5WXF_1 Urokinase-type plasminogen activator chain B (chains U) IIGGEFTTIENQPWFAAIYRRHRGGSVTYVCGGSLISPCWVISATHCFIDYPKKEDYIVY LGRSRLNSNTQGEMKFEVENLILHKDYSADTLAHHNDIALLKIRSKEGRCAQPSRTIQTI ALPSMYNDPQFGTSCEITGFGKEQSTDYLYPEQLKMTVVKLISHRECQQPHYYGSEVTTK MLCAADPQWKTDSCQGDSGGPLVCSLQGRMTLTGIVSWGRGCALKDKPGVYTRVSHFLPW IRSHTKEENGLAL
>5WXF_2 upain-2-2 peptide (chains P) CSWRGLENHAAC
Cleavage of peptidic inhibitors by target protease is caused by peptide conformational transition. Jiang, L., Oldenburg, E., Kromann-Hansen, T. et al. Biochim Biophys Acta (2018) 1862:2017-2023. DOI 10.1016/j.bbagen.2018.06.016 · PubMed
Other PDB entries of the same protein (UniProt P00749 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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