6TKY: DHR2 domain of DOCK10

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.

Method
X-ray diffraction
Resolution
2.55 Å
Organism
Homo sapiens
Chains
4
Atoms
9,543
Mol. weight
148.3 kDa
Released
22 Jan 2020

Explore 6TKY in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

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.

Chain A: 21 helices, 9 β-strands

ElementResiduesLengthSheet
α-helix1696-171318
α-helix1716-173722
α-helix1773-17753
α-helix1777-17804
α-helix1785-17906
α-helix1806-182217
α-helix1826-18283
α-helix1829-184214
α-helix1846-186621
β-strand1876-188385
β-strand1895-190065
α-helix1906-192015
β-strand1926-192945
α-helix1934-19352
α-helix1937-19393
β-strand1945-195285
β-strand1953-195422
α-helix1960-19634
α-helix1967-19704
β-strand1974-1984112
β-strand1996-2009142
β-strand2015-201735
β-strand2018-202692
α-helix2028-204821
α-helix2054-206512
α-helix2074-20807
α-helix2083-20864
α-helix2091-211626
α-helix2121-21233
α-helix2124-214522
Chain B: 21 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix1696-171318
α-helix1716-173621
α-helix1777-17804
α-helix1785-17917
α-helix1806-182217
α-helix1826-18283
α-helix1829-184315
α-helix1846-186419
β-strand1876-188381
β-strand1895-190061
α-helix1906-192116
α-helix1923-19253
β-strand1926-192941
α-helix1934-19352
α-helix1937-19393
β-strand1945-195281
β-strand1953-195422
α-helix1958-19614
β-strand1974-1983102
β-strand1997-2009132
β-strand2015-201731
β-strand2018-202692
α-helix2028-204821
α-helix2054-206512
α-helix2074-20763
α-helix2077-20815
α-helix2083-20864
α-helix2091-211626
α-helix2121-21233
α-helix2124-214522
Chain C: 13 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand3-1083
α-helix12-143
α-helix16-2510
α-helix33-342
β-strand40-4673
β-strand49-5793
α-helix62-643
α-helix68-714
β-strand77-8373
α-helix87-926
α-helix93-975
α-helix98-1047
β-strand110-11563
α-helix117-1193
α-helix123-1319
α-helix136-1383
α-helix139-14911
β-strand154-15633
α-helix165-17612
Chain D: 12 helices, 6 β-strands
ElementResiduesLengthSheet
β-strand3-1084
α-helix16-2510
α-helix33-342
β-strand40-4674
β-strand49-5794
α-helix62-643
α-helix68-714
β-strand77-8374
α-helix87-926
α-helix93-975
α-helix98-1047
β-strand110-11564
α-helix117-1215
α-helix123-1319
α-helix136-1383
α-helix139-14810
β-strand154-15634
α-helix165-17612

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Dedicator of cytokinesis protein 10Bprotein457Homo sapiensQ96BY6 (AlphaFold model)
Cell division control protein 42 homologC, Dprotein188Homo sapiensP60953 (AlphaFold model)
Dedicator of cytokinesis protein 10Aprotein458Homo sapiensQ96BY6 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>6TKY_1 Dedicator of cytokinesis protein 10 (chains B)
STPELRRTWLESMAKIHARNGDLSEAAMCYIHIAALIAEYLKRKGYWKVEKICTASLLSE
DTHPCDSNSLLTTPSGGSMFSMGWPAFLSITPNIKEEGAMKEDSGMQDTPYNENILVEQL
YMCVEFLWKSERYELIADVNKPIIAVFEKQRDFKKLSDLYYDIHRSYLKVAEVVNSEKRL
FGRYYRVAFYGQGFFEEEEGKEYIYKEPKLTGLSEISQRLLKLYADKFGADNVKIIQDSN
KVNPKDLDPKYAYIQVTYVTPFFEEKEIEDRKTDFEMHHNINRFVFETPFTLSGKKHGGV
AEQCKRRTILTTSHLFPYVKKRIQVISQSSTELNPIEVAIDEMSKKVSELNQLCTMEEVD
MIRLQLKLQGSVSVKVNAGPMAYARAFLEETNAKKYPDNQVKLLKEIFRQFADACGQALD
VNERLIKEDQLEYQEELRSHYKDMLSELSTVMNEQIT
Sequence of entity 2 (C, D), FASTA
>6TKY_2 Cell division control protein 42 homolog (chains C, D)
MQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDTAG
QEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQIDLR
DDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALEPP
EPKKSRRC
Sequence of entity 3 (A), FASTA
>6TKY_3 Dedicator of cytokinesis protein 10 (chains A)
STPELRRTWLESMAKIHARNGDLSEAAMCYIHIAALIAEYLKRKGYWKVEKICTASLLSE
DTHPCDSNSLLTTPSGGSMFSMGWPAFLSITPNIKEEGAMKEDSGMQDTPYNENILVEQL
YMCVEFLWKSERYELIADVNKPIIAVFEKQRDFKKLSDLYYDIHRSYLKVAEVVNSEKRL
FGRYYRVAFYGQGFFEEEEGKEYIYKEPKLTGLSEISQRLLKLYADKFGADNVKIIQDSN
KVNPKDLDPKYAYIQVTYVTPFFEEKEIEDRKTDFEMHHNINRFVFETPFTLSGKKHGGV
AEQCKRRTILTTSHLFPYVKKRIQVISQSSTELNPIEVAIDEMSKKVSELNQLCTMEEVD
MIRLQLKLQGSVSVKVNAGPMAYARAFLEETNAKKYPDNQVKLLKEIFRQFADACGQALD
VNERLIKEDQLEYQEELRSHYKDMLSELSTVMNEQITG

Primary citation

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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