Crystal structure of UNC119 in complex with LCK peptide. Determined by X-ray diffraction at 2.0 Å resolution. Released 26 Sept 2018.
Explore 6H6A in 3D Show helices and sheets RCSB PDB PDBe
6H6A contains 19 α-helices and 31 β-strands across 3 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 | 156 | 1 | 3 |
| β-strand | 159-167 | 9 | 2 |
| β-strand | 170-178 | 9 | 2 |
| α-helix | 181 | 1 | |
| β-strand | 182 | 1 | 3 |
| α-helix | 183 | 1 | |
| β-strand | 187-195 | 9 | 1 |
| α-helix | 196-198 | 3 | |
| α-helix | 201-209 | 9 | |
| β-strand | 214-222 | 9 | 2 |
| β-strand | 225-235 | 11 | 2 |
| 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 | 142-151 | 10 | 4 |
| β-strand | 156-167 | 12 | 5 |
| β-strand | 170-182 | 13 | 5 |
| β-strand | 186-195 | 10 | 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 | 62-64 | 3 | |
| α-helix | 79-81 | 3 | |
| β-strand | 87-95 | 9 | 6 |
| β-strand | 101-106 | 6 | 6 |
| β-strand | 128-132 | 5 | 7 |
| α-helix | 135-139 | 5 | |
| β-strand | 142-151 | 10 | 6 |
| β-strand | 156 | 1 | 8 |
| β-strand | 159-167 | 9 | 7 |
| β-strand | 170-178 | 9 | 7 |
| α-helix | 181 | 1 | |
| β-strand | 182 | 1 | 8 |
| α-helix | 183 | 1 | |
| β-strand | 186-195 | 10 | 6 |
| α-helix | 196-198 | 3 | |
| α-helix | 201-209 | 9 | |
| β-strand | 214-222 | 9 | 7 |
| β-strand | 225-235 | 11 | 7 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Protein unc-119 homolog A | D | protein | 182 | Homo sapiens | Q13432 (AlphaFold model) |
| Gly-cys-gly-cys-ser-ser | E, H, K | protein | 10 | Homo sapiens | P06239 (AlphaFold model) |
| Protein unc-119 homolog A | G, J | protein | 182 | Homo sapiens | Q13432 (AlphaFold model) |
>6H6A_1 Protein unc-119 homolog A (chains D) PIGPEDVLGLQRITGDYLCSPEENIYKIDFVRFKIRDMDSGTVLFEIKKPPVSERLPINR RDKDPNAGRFVRYQFTPAFLRLRQVGATVEFTVGDKPVNNFRMIERHYFRNQLLKSFDFH FGFCIPSSKNTCEHIYDFPPLSEELISEMIRHPYETQSDSFYFVDDRLVMHNKADYSYSG TP
>6H6A_2 GLY-CYS-GLY-CYS-SER-SER (chains E, H, K) GCGCSSHPED
>6H6A_3 Protein unc-119 homolog A (chains G, J) PIGPEDVLGLQRITGDYLCSPEENIYKIDFVRFKIRDMDSGTVLFEIKKPPVSERLPINR RDLDPNAGRFVRYQFTPAFLRLRQVGATVEFTVGDKPVNNFRMIERHYFRNQLLKSFDFH FGFCIPSSKNTCEHIYDFPPLSEELISEMIRHPYETQSDSFYFVDDRLVMHNKADYSYSG TP
| ID | Name | Formula | Copies |
|---|---|---|---|
| 15P | Polyethylene glycol (N=34) | C69 H140 O35 | 1 |
| MYR | Myristic acid | C14 H28 O2 | 3 |
| PO4 | Phosphate ion | O4 P | 2 |
Water and common crystallization additives (GOL) are not listed.
The Ciliary Machinery Is Repurposed for T Cell Immune Synapse Trafficking of LCK. Stephen, L.A., ElMaghloob, Y., McIlwraith, M.J. et al. Dev Cell (2018) 47:122-132.e4. DOI 10.1016/j.devcel.2018.08.012 · 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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