Crystal structure of UNC119 in complex with Squarunkin A. Determined by X-ray diffraction at 2.21 Å resolution. Released 15 Jan 2025.
Explore 9GKG in 3D Show helices and sheets RCSB PDB PDBe
9GKG contains 38 α-helices and 64 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 | 62-65 | 4 | |
| α-helix | 79-81 | 3 | |
| β-strand | 87-95 | 9 | 4 |
| β-strand | 101-106 | 6 | 4 |
| β-strand | 128-132 | 5 | 5 |
| α-helix | 135-139 | 5 | |
| β-strand | 142-150 | 9 | 4 |
| β-strand | 156 | 1 | 6 |
| β-strand | 159-167 | 9 | 5 |
| β-strand | 170-178 | 9 | 5 |
| α-helix | 181 | 1 | |
| β-strand | 182 | 1 | 6 |
| α-helix | 183 | 1 | |
| β-strand | 187-195 | 9 | 4 |
| α-helix | 196-198 | 3 | |
| α-helix | 201-209 | 9 | |
| β-strand | 214-222 | 9 | 5 |
| β-strand | 225-235 | 11 | 5 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 62-65 | 4 | |
| α-helix | 79-81 | 3 | |
| β-strand | 87-95 | 9 | 7 |
| β-strand | 101-106 | 6 | 7 |
| β-strand | 128-132 | 5 | 8 |
| α-helix | 135-139 | 5 | |
| β-strand | 142-150 | 9 | 7 |
| β-strand | 156 | 1 | 9 |
| β-strand | 160-167 | 8 | 8 |
| β-strand | 170-178 | 9 | 8 |
| β-strand | 182 | 1 | 9 |
| β-strand | 187-195 | 9 | 7 |
| α-helix | 196-198 | 3 | |
| α-helix | 201-209 | 9 | |
| β-strand | 214-222 | 9 | 8 |
| β-strand | 225-235 | 11 | 8 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 62-65 | 4 | |
| α-helix | 79-81 | 3 | |
| β-strand | 87-95 | 9 | 10 |
| β-strand | 101-106 | 6 | 10 |
| β-strand | 128-132 | 5 | 11 |
| α-helix | 135-139 | 5 | |
| β-strand | 142-150 | 9 | 10 |
| β-strand | 156 | 1 | 12 |
| β-strand | 160-167 | 8 | 11 |
| β-strand | 170-178 | 9 | 11 |
| α-helix | 181 | 1 | |
| β-strand | 182 | 1 | 12 |
| α-helix | 183 | 1 | |
| β-strand | 187-195 | 9 | 10 |
| α-helix | 196-198 | 3 | |
| α-helix | 201-209 | 9 | |
| β-strand | 214-222 | 9 | 11 |
| β-strand | 225-235 | 11 | 11 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 62-65 | 4 | |
| α-helix | 79-81 | 3 | |
| β-strand | 87-95 | 9 | 16 |
| β-strand | 101-106 | 6 | 16 |
| β-strand | 128-132 | 5 | 17 |
| α-helix | 135-139 | 5 | |
| β-strand | 142-150 | 9 | 16 |
| β-strand | 160-167 | 8 | 17 |
| β-strand | 170-178 | 9 | 17 |
| β-strand | 187-195 | 9 | 16 |
| α-helix | 196-198 | 3 | |
| α-helix | 201-209 | 9 | |
| β-strand | 214-222 | 9 | 17 |
| β-strand | 225-235 | 11 | 17 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein unc-119 homolog A | A, B, C, D, E, K | protein | 182 | Homo sapiens | Q13432 (AlphaFold model) |
>9GKG_1 Protein unc-119 homolog A (chains A, B, C, D, E, K) PIGPEDVLGLQRITGDYLCSPEENIYKIDFVRFKIRDMDSGTVLFEIKKPPVSERLPINR RDLDPNAGRFVRYQFTPAFLRLRQVGATVEFTVGDKPVNNFRMIERHYFRNQLLKSFDFH FGFCIPSSKNTCEHIYDFPPLSEELISEMIRHPYETQSDSFYFVDDRLVMHNKADYSYSG TP
| ID | Name | Formula | Copies |
|---|---|---|---|
| LRX | squarunkin A | C25 H32 F3 N5 O4 | 2 |
Water and common crystallization additives (EDO) are not listed.
UNC119 regulates T-cell receptor signalling in primary T cells and T acute lymphocytic leukaemia. Samarakoon, Y., Yelland, T., Garcia-Gonzalez, E. et al. Life Sci Alliance (2025) 8. DOI 10.26508/lsa.202403066 · 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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