Structure of Unc119-inhibitor complex. Determined by X-ray diffraction at 2.3 Å resolution. Released 26 Jul 2023.
Explore 7UMO in 3D Show helices and sheets RCSB PDB PDBe
7UMO contains 32 α-helices and 60 β-strands across 6 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 |
|---|---|---|---|
| α-helix | 62-64 | 3 | |
| α-helix | 79-81 | 3 | |
| β-strand | 87-95 | 9 | 1 |
| β-strand | 101-106 | 6 | 1 |
| β-strand | 128-132 | 5 | 2 |
| α-helix | 135-139 | 5 | |
| β-strand | 142-150 | 9 | 1 |
| β-strand | 159-167 | 9 | 2 |
| β-strand | 170-178 | 9 | 2 |
| β-strand | 187-195 | 9 | 1 |
| α-helix | 196-200 | 5 | |
| α-helix | 201-209 | 9 | |
| β-strand | 214-222 | 9 | 2 |
| β-strand | 225-235 | 11 | 2 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 62-66 | 5 | |
| α-helix | 79-81 | 3 | |
| β-strand | 87-95 | 9 | 5 |
| β-strand | 101-106 | 6 | 5 |
| β-strand | 128-132 | 5 | 6 |
| α-helix | 135-139 | 5 | |
| β-strand | 142-150 | 9 | 5 |
| β-strand | 156 | 1 | 7 |
| β-strand | 160-167 | 8 | 6 |
| β-strand | 171-178 | 8 | 6 |
| β-strand | 182 | 1 | 7 |
| β-strand | 187-195 | 9 | 5 |
| α-helix | 196-198 | 3 | |
| α-helix | 201-209 | 9 | |
| β-strand | 214-222 | 9 | 6 |
| β-strand | 225-235 | 11 | 6 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 62-65 | 4 | |
| α-helix | 79-81 | 3 | |
| β-strand | 87-95 | 9 | 8 |
| β-strand | 101-106 | 6 | 8 |
| β-strand | 128-132 | 5 | 9 |
| α-helix | 135-139 | 5 | |
| β-strand | 142-150 | 9 | 8 |
| β-strand | 156 | 1 | 10 |
| β-strand | 160-167 | 8 | 9 |
| β-strand | 171-178 | 8 | 9 |
| β-strand | 182 | 1 | 10 |
| β-strand | 187-195 | 9 | 8 |
| α-helix | 196-198 | 3 | |
| α-helix | 201-209 | 9 | |
| β-strand | 214-222 | 9 | 9 |
| β-strand | 225-235 | 11 | 9 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 62-66 | 5 | |
| α-helix | 79-81 | 3 | |
| β-strand | 87-95 | 9 | 11 |
| β-strand | 101-106 | 6 | 11 |
| β-strand | 128-132 | 5 | 12 |
| α-helix | 135-139 | 5 | |
| β-strand | 142-150 | 9 | 11 |
| β-strand | 156 | 1 | 13 |
| β-strand | 159-167 | 9 | 12 |
| β-strand | 170-178 | 9 | 12 |
| α-helix | 181 | 1 | |
| β-strand | 182 | 1 | 13 |
| α-helix | 183 | 1 | |
| β-strand | 187-195 | 9 | 11 |
| α-helix | 196-198 | 3 | |
| α-helix | 201-209 | 9 | |
| β-strand | 214-222 | 9 | 12 |
| β-strand | 225-235 | 11 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 62-64 | 3 | |
| α-helix | 79-81 | 3 | |
| β-strand | 87-95 | 9 | 14 |
| β-strand | 101-106 | 6 | 14 |
| β-strand | 128-132 | 5 | 15 |
| α-helix | 135-139 | 5 | |
| β-strand | 142-150 | 9 | 14 |
| α-helix | 155-156 | 2 | |
| β-strand | 159-167 | 9 | 15 |
| β-strand | 171-178 | 8 | 15 |
| β-strand | 187-195 | 9 | 14 |
| α-helix | 201-209 | 9 | |
| β-strand | 214-222 | 9 | 15 |
| β-strand | 225-235 | 11 | 15 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein unc-119 homolog A | A, B, C, D, E, F | protein | 196 | Homo sapiens | Q13432 (AlphaFold model) |
>7UMO_1 Protein unc-119 homolog A (chains A, B, C, D, E, F) MGSSHHHHHHSSKQPIGPEDVLGLQRITGDYLCSPEENIYKIDFVRFKIRDMDSGTVLFE IKKPPVSERLPINRRDLDPNAGRFVRYQFTPAFLRLRQVGATVEFTVGDKPVNNFRMIER HYFRNQLLKSFDFHFGFCIPSSKNTCEHIYDFPPLSEELISEMIRHPYETQSDSFYFVDD RLVMHNKADYSYSGTP
| ID | Name | Formula | Copies |
|---|---|---|---|
| NT6 | (3s,5s,7s)-N-(4,5-dichloropyridin-2-yl)adamantane-1-carboxamide | C16 H18 Cl2 N2 O | 6 |
Water and common crystallization additives (GOL) are not listed.
Insulin sensitization by small molecules enhancing GLUT4 translocation. Yin, T.C., Van Vranken, J.G., Srivastava, D. et al. Cell Chem Biol (2023) 30:933-942.e6. DOI 10.1016/j.chembiol.2023.06.012 · PubMed
Other PDB entries of the same protein (UniProt Q13432 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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