2WM9: Complex between DOCK9 and Cdc42

Structure of the complex between DOCK9 and Cdc42. Determined by X-ray diffraction at 2.2 Å resolution. Released 22 Sept 2009.

Method: X-ray diffraction
Resolution: 2.2 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 4,791
Mol. weight: 71.48 kDa
Released: 22 Sept 2009

Explore 2WM9 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

2WM9 contains 35 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: 22 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	6-24	19
α-helix	27-47	21
α-helix	55-58	4
α-helix	63-68	6
α-helix	84-100	17
α-helix	104-106	3
α-helix	107-111	5
α-helix	115-120	6
α-helix	124-147	24
β-strand	154-161	8	1
α-helix	163-166	4
α-helix	167-169	3
β-strand	173-178	6	1
α-helix	184-199	16
α-helix	201-203	3
β-strand	204-207	4	1
α-helix	212-213	2
α-helix	215-217	3
β-strand	223-230	8	1
β-strand	231-232	2	2
α-helix	236-241	6
α-helix	246-248	3
β-strand	252-261	10	2
β-strand	275-287	13	2
β-strand	293-295	3	1
β-strand	296-304	9	2
α-helix	306-326	21
α-helix	332-343	12
α-helix	352-358	7
α-helix	372-396	25
α-helix	403-423	21

Chain B: 13 helices, 6 β-strands

Element	Residues	Length	Sheet
α-helix	0-2	3
β-strand	3-10	8	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	117-120	4
α-helix	123-130	8
α-helix	136-138	3
α-helix	139-149	11
β-strand	154-156	3	3
α-helix	165-176	12

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Dedicator of cytokinesis protein 9	A	protein	428	HOMO SAPIENS	Q9BZ29 (AlphaFold model)
Cell division control protein 42 homolog	B	protein	190	HOMO SAPIENS	P60953 (AlphaFold model)

Sequence of entity 1 (A), FASTA

>2WM9_1 DEDICATOR OF CYTOKINESIS PROTEIN 9 (chains A)
KSYASTPELRKTWLDSMARIHVKNGDLSEAAMCYVHVTALVAEYLTRKGVFRQGCTAFRV
ITPNIDEEASMMEDVGMQDVHFNEDVLMELLEQCADGLWKAERYELIADIYKLIIPIYEK
RRDFERLAHLYDTLHRAYSKVTEVMHSGRRLLGTYFRVAFFGQGFFEDEDGKEYIYKEPK
LTPLSEISQRLLKLYSDKFGSENVKMIQDSGKVNPKDLDSKYAYIQVTHVIPFFDEKELQ
ERKTEFERSHNIRRFMFEMPFTQTGKRQGGVEEQCKRRTILTAIHCFPYVKKRIPVMYQH
HTDLNPIEVAIDEMSKKVAELRQLCSSAEVDMIKLQLKLQGSVSVQVNAGPLAYARAFLD
DTNTKRYPDNKVKLLKEVFRQFVEACGQALAVNERLIKEDQLEYQEEMKANYREMAKELS
EIMHEQLG

Sequence of entity 2 (B), FASTA

>2WM9_2 CELL DIVISION CONTROL PROTEIN 42 HOMOLOG (chains B)
SHMQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDT
AGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQID
LRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALE
PPEPKKSRRC

Primary citation

Activation of Rho Gtpases by Dock Exchange Factors is Mediated by a Nucleotide Sensor. Yang, J., Zhang, Z., Roe, S.M. et al. Science (2009) 325:1398. DOI 10.1126/SCIENCE.1174468 · PubMed

Other PDB entries of the same protein (UniProt Q9BZ29 (AlphaFold model), which also has an AlphaFold model), best resolution first:

2WMO 2.2 Å, Structure of the complex between DOCK9 and Cdc42.
2WMN 2.39 Å, Structure of the complex between DOCK9 and Cdc42-GDP.
1WG7 Solution structure of pleckstrin homology domain from human KIAA1058 protein

Browse structure collections

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