8I5F: DHR-2 domain of DOCK10

Crystal structure of the DHR-2 domain of DOCK10 in complex with Cdc42 (T17N mutant). Determined by X-ray diffraction at 2.8 Å resolution. Released 15 Mar 2023.

Method: X-ray diffraction
Resolution: 2.8 Å
Organisms: Mus musculus, Homo sapiens
Chains: 4
Atoms: 9,921
Mol. weight: 156.93 kDa
Released: 15 Mar 2023

Explore 8I5F in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8I5F contains 67 α-helices and 31 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, 10 β-strands

Element	Residues	Length	Sheet
α-helix	1680-1690	11
α-helix	1696-1713	18
α-helix	1716-1737	22
α-helix	1773-1775	3
α-helix	1778-1780	3
α-helix	1785-1791	7
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	1
β-strand	1892	1	1
β-strand	1895-1900	6	1
α-helix	1906-1921	16
β-strand	1926-1929	4	1
α-helix	1934-1936	3
α-helix	1937-1939	3
β-strand	1945-1952	8	1
β-strand	1953-1954	2	2
α-helix	1958-1963	6
α-helix	1967-1971	5
β-strand	1974-1984	11	2
β-strand	1996-2009	14	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	2073-2081	9
α-helix	2083-2088	6
α-helix	2091-2118	28
α-helix	2124-2145	22

Chain B: 22 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	1680-1690	11
α-helix	1696-1712	17
α-helix	1716-1736	21
α-helix	1773-1775	3
α-helix	1777-1780	4
α-helix	1785-1792	8
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	4
β-strand	1895-1900	6	4
α-helix	1906-1921	16
β-strand	1926-1929	4	4
α-helix	1934-1936	3
α-helix	1937-1939	3
β-strand	1945-1952	8	4
β-strand	1953-1954	2	5
α-helix	1958-1963	6
α-helix	1967-1971	5
β-strand	1974-1984	11	5
β-strand	1996-2009	14	5
β-strand	2015-2017	3	4
β-strand	2018-2026	9	5
α-helix	2028-2048	21
α-helix	2054-2065	12
α-helix	2073-2076	4
α-helix	2077-2081	5
α-helix	2083-2088	6
α-helix	2091-2118	28
α-helix	2124-2145	22

Chain C: 12 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	4-10	7	3
α-helix	16-25	10
α-helix	29-31	3
α-helix	32-34	3
β-strand	40-46	7	3
β-strand	49-57	9	3
α-helix	58-59	2
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	119-121	3
α-helix	123-131	9
α-helix	139-148	10
β-strand	154-156	3	3
α-helix	165-176	12

Chain D: 12 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	3-10	8	6
α-helix	16-24	9
α-helix	29-31	3
β-strand	40-46	7	6
β-strand	49-57	9	6
α-helix	62-66	5
α-helix	68-71	4
β-strand	77-83	7	6
α-helix	87-92	6
α-helix	93-97	5
α-helix	98-104	7
β-strand	110-115	6	6
α-helix	117-121	5
α-helix	123-130	8
α-helix	136-138	3
α-helix	139-146	8
β-strand	154-156	3	6
α-helix	165-175	11

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Dedicator of cytokinesis protein 10	A, B	protein	494	Mus musculus	Q8BZN6 (AlphaFold model)
Cell division control protein 42 homolog	C, D	protein	195	Homo sapiens	P60953 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>8I5F_1 Dedicator of cytokinesis protein 10 (chains A, B)
GSSGSSGVLMATAQMKEHEKDPEMLVDLQYSLANSYASTPELRRTWLESMAKIHARNGDL
SEAAMCYIHIAALIAEYLKRKGYWKMEKICTPPLLPEDTQPCDSNLLLTTPGGGSMFSMG
WPAFLSITPNIKEEGAMKEDSGMQDTPYNENILVEQLYMCVEFLWKSERYELIADVNKPI
IAVFEKQRDFKKLSDLYYDIHRSYLKVAEVVNSEKRLFGRYYRVAFYGQGFFEEEEGKEY
IYKEPKLTGLSEISQRLLKLYADKFGADNVKIIQDSNKVNPKDLDPKYAYIQVTYVTPFF
EEKEIEDRKTDFEMHHNINRFVFETPFTLSGKKHGGVAEQCKRRTVLTTSHLFPYVKKRI
QVISQSSTELNPIEVAIDEMSRKVSELNQLCTTEEVDMIRLQLKLQGSVSVKVNAGPMAY
ARAFLEETNAKKYPDNQVKLLKEIFRQFADACGQALDVNERLIKEDQLEYQEELRSHYKD
MLSELSAIMNEQIT

Sequence of entity 2 (C, D), FASTA

>8I5F_2 Cell division control protein 42 homolog (chains C, D)
GSSGSSGMQTIKCVVVGDGAVGKNCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTL
GLFDTAGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLV
GTQIDLRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAI
LAALEPPEPKKSRRS

Primary citation

Structural basis for the dual GTPase specificity of the DOCK10 guanine nucleotide exchange factor. Kukimoto-Niino, M., Ihara, K., Mishima-Tsumagari, C. et al. Biochem Biophys Res Commun (2023) 653:12-20. DOI 10.1016/j.bbrc.2023.02.054 · PubMed

Other PDB entries of the same protein (UniProt Q8BZN6 (AlphaFold model), which also has an AlphaFold model), best resolution first:

8I5V 1.73 Å, DOCK10 mutant L1903Y complexed with Rac1
8I5W 2.43 Å, Crystal structure of the DHR-2 domain of DOCK10 in complex with Rac1

Browse structure collections

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