Crystal structure of the DHR2 domain of DOCK10 in complex with CDC42. Determined by X-ray diffraction at 2.55 Å resolution. Released 22 Jan 2020.
Explore 6TKY in 3D Show helices and sheets RCSB PDB PDBe
6TKY contains 67 α-helices and 30 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 |
|---|---|---|---|
| α-helix | 1696-1713 | 18 | |
| α-helix | 1716-1737 | 22 | |
| α-helix | 1773-1775 | 3 | |
| α-helix | 1777-1780 | 4 | |
| α-helix | 1785-1790 | 6 | |
| α-helix | 1806-1822 | 17 | |
| α-helix | 1826-1828 | 3 | |
| α-helix | 1829-1842 | 14 | |
| α-helix | 1846-1866 | 21 | |
| β-strand | 1876-1883 | 8 | 5 |
| β-strand | 1895-1900 | 6 | 5 |
| α-helix | 1906-1920 | 15 | |
| β-strand | 1926-1929 | 4 | 5 |
| α-helix | 1934-1935 | 2 | |
| α-helix | 1937-1939 | 3 | |
| β-strand | 1945-1952 | 8 | 5 |
| β-strand | 1953-1954 | 2 | 2 |
| α-helix | 1960-1963 | 4 | |
| α-helix | 1967-1970 | 4 | |
| β-strand | 1974-1984 | 11 | 2 |
| β-strand | 1996-2009 | 14 | 2 |
| β-strand | 2015-2017 | 3 | 5 |
| β-strand | 2018-2026 | 9 | 2 |
| α-helix | 2028-2048 | 21 | |
| α-helix | 2054-2065 | 12 | |
| α-helix | 2074-2080 | 7 | |
| α-helix | 2083-2086 | 4 | |
| α-helix | 2091-2116 | 26 | |
| α-helix | 2121-2123 | 3 | |
| α-helix | 2124-2145 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| α-helix | 1696-1713 | 18 | |
| α-helix | 1716-1736 | 21 | |
| α-helix | 1777-1780 | 4 | |
| α-helix | 1785-1791 | 7 | |
| α-helix | 1806-1822 | 17 | |
| α-helix | 1826-1828 | 3 | |
| α-helix | 1829-1843 | 15 | |
| α-helix | 1846-1864 | 19 | |
| β-strand | 1876-1883 | 8 | 1 |
| β-strand | 1895-1900 | 6 | 1 |
| α-helix | 1906-1921 | 16 | |
| α-helix | 1923-1925 | 3 | |
| β-strand | 1926-1929 | 4 | 1 |
| α-helix | 1934-1935 | 2 | |
| α-helix | 1937-1939 | 3 | |
| β-strand | 1945-1952 | 8 | 1 |
| β-strand | 1953-1954 | 2 | 2 |
| α-helix | 1958-1961 | 4 | |
| β-strand | 1974-1983 | 10 | 2 |
| β-strand | 1997-2009 | 13 | 2 |
| β-strand | 2015-2017 | 3 | 1 |
| β-strand | 2018-2026 | 9 | 2 |
| α-helix | 2028-2048 | 21 | |
| α-helix | 2054-2065 | 12 | |
| α-helix | 2074-2076 | 3 | |
| α-helix | 2077-2081 | 5 | |
| α-helix | 2083-2086 | 4 | |
| α-helix | 2091-2116 | 26 | |
| α-helix | 2121-2123 | 3 | |
| α-helix | 2124-2145 | 22 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-10 | 8 | 3 |
| α-helix | 12-14 | 3 | |
| α-helix | 16-25 | 10 | |
| α-helix | 33-34 | 2 | |
| β-strand | 40-46 | 7 | 3 |
| β-strand | 49-57 | 9 | 3 |
| α-helix | 62-64 | 3 | |
| α-helix | 68-71 | 4 | |
| β-strand | 77-83 | 7 | 3 |
| α-helix | 87-92 | 6 | |
| α-helix | 93-97 | 5 | |
| α-helix | 98-104 | 7 | |
| β-strand | 110-115 | 6 | 3 |
| α-helix | 117-119 | 3 | |
| α-helix | 123-131 | 9 | |
| α-helix | 136-138 | 3 | |
| α-helix | 139-149 | 11 | |
| β-strand | 154-156 | 3 | 3 |
| α-helix | 165-176 | 12 |
| Element | Residues | Length | Sheet |
|---|---|---|---|
| β-strand | 3-10 | 8 | 4 |
| α-helix | 16-25 | 10 | |
| α-helix | 33-34 | 2 | |
| β-strand | 40-46 | 7 | 4 |
| β-strand | 49-57 | 9 | 4 |
| α-helix | 62-64 | 3 | |
| α-helix | 68-71 | 4 | |
| β-strand | 77-83 | 7 | 4 |
| α-helix | 87-92 | 6 | |
| α-helix | 93-97 | 5 | |
| α-helix | 98-104 | 7 | |
| β-strand | 110-115 | 6 | 4 |
| α-helix | 117-121 | 5 | |
| α-helix | 123-131 | 9 | |
| α-helix | 136-138 | 3 | |
| α-helix | 139-148 | 10 | |
| β-strand | 154-156 | 3 | 4 |
| α-helix | 165-176 | 12 |
| Molecule | Chains | Type | Length | Organism | UniProt |
|---|---|---|---|---|---|
| Dedicator of cytokinesis protein 10 | B | protein | 457 | Homo sapiens | Q96BY6 (AlphaFold model) |
| Cell division control protein 42 homolog | C, D | protein | 188 | Homo sapiens | P60953 (AlphaFold model) |
| Dedicator of cytokinesis protein 10 | A | protein | 458 | Homo sapiens | Q96BY6 (AlphaFold model) |
>6TKY_1 Dedicator of cytokinesis protein 10 (chains B) STPELRRTWLESMAKIHARNGDLSEAAMCYIHIAALIAEYLKRKGYWKVEKICTASLLSE DTHPCDSNSLLTTPSGGSMFSMGWPAFLSITPNIKEEGAMKEDSGMQDTPYNENILVEQL YMCVEFLWKSERYELIADVNKPIIAVFEKQRDFKKLSDLYYDIHRSYLKVAEVVNSEKRL FGRYYRVAFYGQGFFEEEEGKEYIYKEPKLTGLSEISQRLLKLYADKFGADNVKIIQDSN KVNPKDLDPKYAYIQVTYVTPFFEEKEIEDRKTDFEMHHNINRFVFETPFTLSGKKHGGV AEQCKRRTILTTSHLFPYVKKRIQVISQSSTELNPIEVAIDEMSKKVSELNQLCTMEEVD MIRLQLKLQGSVSVKVNAGPMAYARAFLEETNAKKYPDNQVKLLKEIFRQFADACGQALD VNERLIKEDQLEYQEELRSHYKDMLSELSTVMNEQIT
>6TKY_2 Cell division control protein 42 homolog (chains C, D) MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAG QEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLR DDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPP EPKKSRRC
>6TKY_3 Dedicator of cytokinesis protein 10 (chains A) STPELRRTWLESMAKIHARNGDLSEAAMCYIHIAALIAEYLKRKGYWKVEKICTASLLSE DTHPCDSNSLLTTPSGGSMFSMGWPAFLSITPNIKEEGAMKEDSGMQDTPYNENILVEQL YMCVEFLWKSERYELIADVNKPIIAVFEKQRDFKKLSDLYYDIHRSYLKVAEVVNSEKRL FGRYYRVAFYGQGFFEEEEGKEYIYKEPKLTGLSEISQRLLKLYADKFGADNVKIIQDSN KVNPKDLDPKYAYIQVTYVTPFFEEKEIEDRKTDFEMHHNINRFVFETPFTLSGKKHGGV AEQCKRRTILTTSHLFPYVKKRIQVISQSSTELNPIEVAIDEMSKKVSELNQLCTMEEVD MIRLQLKLQGSVSVKVNAGPMAYARAFLEETNAKKYPDNQVKLLKEIFRQFADACGQALD VNERLIKEDQLEYQEELRSHYKDMLSELSTVMNEQITG
Structural basis for CDC42 and RAC activation by the dual specificity GEF DOCK10. Fan, D., Yang, J., Cronin, N. et al. bioRxiv (2022). DOI 10.1101/2022.06.15.496229
Other PDB entries of the same protein (UniProt Q96BY6 (AlphaFold model), which also has an AlphaFold model), best resolution first:
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