6TM1: DHR2 domain of DOCK10

Crystal structure of the DHR2 domain of DOCK10 in complex with RAC3. Determined by X-ray diffraction at 3.71 Å resolution. Released 22 Jan 2020.

Method
X-ray diffraction
Resolution
3.71 Å
Organism
Homo sapiens
Chains
3
Atoms
6,775
Mol. weight
127.52 kDa
Released
22 Jan 2020

Explore 6TM1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6TM1 contains 41 α-helices and 28 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.

Chain A: 8 helices, 10 β-strands

ElementResiduesLengthSheet
β-strand413
β-strand614
β-strand7-825
α-helix16-249
β-strand41-4553
β-strand50-5453
β-strand56-5725
α-helix69-713
β-strand7714
β-strand78-8366
α-helix87-9610
α-helix98-1014
β-strand110-11566
α-helix118-1214
α-helix123-13210
α-helix139-14810
β-strand155-15626
α-helix167-17711
Chain B: 15 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix1696-171217
α-helix1716-173621
α-helix1778-17803
α-helix1785-17906
α-helix1806-182217
α-helix1830-184314
α-helix1847-186418
β-strand1877-188371
β-strand1895-189951
α-helix1906-191813
β-strand192711
β-strand1946-195161
β-strand1953-195422
α-helix1960-19634
β-strand1976-198272
β-strand1998-200472
α-helix20081
β-strand201711
β-strand2022-202652
α-helix2030-204415
α-helix2054-206411
α-helix2075-20806
α-helix2093-211523
α-helix2123-214523
Chain C: 18 helices, 9 β-strands
ElementResiduesLengthSheet
α-helix1699-171315
α-helix1716-173621
α-helix1785-17873
α-helix1806-182318
α-helix1826-18283
α-helix1829-18324
α-helix1836-18427
α-helix1847-186620
β-strand1876-188277
β-strand1895-190067
α-helix1907-191711
β-strand1947-195267
β-strand195318
α-helix1960-19634
α-helix1968-19714
β-strand1974-197968
β-strand1998-2009128
β-strand2015-201737
β-strand2018-202038
β-strand2023-202648
α-helix2028-204821
α-helix2055-20639
α-helix2074-20785
α-helix2099-21068
α-helix2107-21093
α-helix2110-21189
α-helix2126-213712

Molecules and chains

MoleculeChainsTypeLengthOrganismUniProt
Dedicator of cytokinesis protein 10Bprotein457Homo sapiensQ96BY6 (AlphaFold model)
Ras-related C3 botulinum toxin substrate 3Aprotein192Homo sapiensP60763 (AlphaFold model)
Dedicator of cytokinesis protein 10Cprotein458Homo sapiensQ96BY6 (AlphaFold model)
Sequence of entity 1 (B), FASTA
>6TM1_1 Dedicator of cytokinesis protein 10 (chains B)
STPELRRTWLESMAKIHARNGDLSEAAMCYIHIAALIAEYLKRKGYWKVEKICTASLLSE
DTHPCDSNSLLTTPSGGSMFSMGWPAFLSITPNIKEEGAMKEDSGMQDTPYNENILVEQL
YMCVEFLWKSERYELIADVNKPIIAVFEKQRDFKKLSDLYYDIHRSYLKVAEVVNSEKRL
FGRYYRVAFYGQGFFEEEEGKEYIYKEPKLTGLSEISQRLLKLYADKFGADNVKIIQDSN
KVNPKDLDPKYAYIQVTYVTPFFEEKEIEDRKTDFEMHHNINRFVFETPFTLSGKKHGGV
AEQCKRRTILTTSHLFPYVKKRIQVISQSSTELNPIEVAIDEMSKKVSELNQLCTMEEVD
MIRLQLKLQGSVSVKVNAGPMAYARAFLEETNAKKYPDNQVKLLKEIFRQFADACGQALD
VNERLIKEDQLEYQEELRSHYKDMLSELSTVMNEQIT
Sequence of entity 2 (A), FASTA
>6TM1_2 Ras-related C3 botulinum toxin substrate 3 (chains A)
MQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNLGLWDTAG
QEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPHTPILLVGTKLDLR
DDKDTIERLRDKKLAPITYPQGLAMAREIGSVKYLECSALTQRGLKTVFDEAIRAVLCPP
PVKKPGKKCTVF
Sequence of entity 3 (C), FASTA
>6TM1_3 Dedicator of cytokinesis protein 10 (chains C)
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:

Browse structure collections

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