8I5V: DOCK10 mutant L1903Y

DOCK10 mutant L1903Y complexed with Rac1. Determined by X-ray diffraction at 1.73 Å resolution. Released 15 Mar 2023.

Method: X-ray diffraction
Resolution: 1.73 Å
Organisms: Mus musculus, Homo sapiens
Chains: 2
Atoms: 4,169
Mol. weight: 52.98 kDa
Released: 15 Mar 2023

Explore 8I5V in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

8I5V contains 25 α-helices and 15 β-strands across 2 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: 13 helices, 9 β-strands

Element	Residues	Length	Sheet
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	1958-1963	6
α-helix	1967-1969	3
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	2074-2080	7
α-helix	2086-2087	2
α-helix	2091-2118	28
α-helix	2121-2123	3
α-helix	2124-2145	22

Chain B: 12 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	2-10	9	3
α-helix	16-25	10
α-helix	29-31	3
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	123-130	8
α-helix	136-138	3
α-helix	139-149	11
β-strand	153-156	4	3
α-helix	165-174	10

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Dedicator of cytokinesis protein 10	A	protein	282	Mus musculus	Q8BZN6 (AlphaFold model)
Ras-related C3 botulinum toxin substrate 1	B	protein	184	Homo sapiens	P63000 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>8I5V_1 Dedicator of cytokinesis protein 10 (chains A)
GSSGSSGRYYRVAFYGQGFFEEEEGKEYIYKEPKYTGLSEISQRLLKLYADKFGADNVKI
IQDSNKVNPKDLDPKYAYIQVTYVTPFFEEKEIEDRKTDFEMHHNINRFVFETPFTLSGK
KHGGVAEQCKRRTVLTTSHLFPYVKKRIQVISQSSTELNPIEVAIDEMSRKVSELNQLCT
TEEVDMIRLQLKLQGSVSVKVNAGPMAYARAFLEETNAKKYPDNQVKLLKEIFRQFADAC
GQALDVNERLIKEDQLEYQEELRSHYKDMLSELSAIMNEQIT

Sequence of entity 2 (B), FASTA

>8I5V_2 Ras-related C3 botulinum toxin substrate 1 (chains B)
GSSGSSGMQAIKCVVVGDGAVGKTCLLISYTTNAFPGEYIPTVFDNYSANVMVDGKPVNL
GLWDTAGQEDYDRLRPLSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILV
GTKLDLRDDKDTIEKLKEKKLTPITYPQGLAMAKEIGAVKYLECSALTQRGLKTVFDEAI
RAVL

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:

8I5W 2.43 Å, Crystal structure of the DHR-2 domain of DOCK10 in complex with Rac1
8I5F 2.8 Å, Crystal structure of the DHR-2 domain of DOCK10 in complex with Cdc42 (T17N mutant)

Browse structure collections

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