2WMN: Complex between DOCK9 and Cdc42-GDP

Structure of the complex between DOCK9 and Cdc42-GDP. Determined by X-ray diffraction at 2.39 Å resolution. Released 22 Sept 2009.

Method: X-ray diffraction
Resolution: 2.39 Å
Organism: HOMO SAPIENS
Chains: 2
Atoms: 4,751
Mol. weight: 71.65 kDa
Ligands: GDP
Released: 22 Sept 2009

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

Secondary structure: helices and β-sheets

2WMN contains 33 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: 20 helices, 9 β-strands

Element	Residues	Length	Sheet
α-helix	6-24	19
α-helix	27-47	21
α-helix	63-67	5
α-helix	84-100	17
α-helix	104-106	3
α-helix	107-120	14
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	215-217	3
β-strand	223-230	8	1
β-strand	231-232	2	2
α-helix	236-241	6
α-helix	247-249	3
β-strand	252-261	10	2
α-helix	271-273	3
β-strand	275-287	13	2
β-strand	293-295	3	1
β-strand	296-304	9	2
α-helix	306-325	20
α-helix	332-343	12
α-helix	352-358	7
α-helix	372-394	23
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	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	117-121	5
α-helix	123-130	8
α-helix	136-138	3
α-helix	139-148	10
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

>2WMN_1 DEDICATOR OF CYTOKINESIS PROTEIN 9 (chains A)
KSYASTPELRKTWLDSMARIHVKNGDLSEAAMCYVHVTALVAEYLTRKGVFRQGCTAFRV
ITPNIDEEASMMEDVGMQDVHFNEDVLMELLEQCADGLWKAERYELIADIYKLIIPIYEK
RRDFERLAHLYDTLHRAYSKVTEVMHSGRRLLGTYFRVAFFGQGFFEDEDGKEYIYKEPK
LTPLSEISQRLLKLYSDKFGSENVKMIQDSGKVNPKDLDSKYAYIQVTHVIPFFDEKELQ
ERKTEFERSHNIRRFMFEMPFTQTGKRQGGVEEQCKRRTILTAIHCFPYVKKRIPVMYQH
HTDLNPIEVAIDEMSKKVAELRQLCSSAEVDMIKLQLKLQGSVSVQVNAGPLAYARAFLD
DTNTKRYPDNKVKLLKEVFRQFVEACGQALAVNERLIKEDQLEYQEEMKANYREMAKELS
EIMHEQLG

Sequence of entity 2 (B), FASTA

>2WMN_2 CELL DIVISION CONTROL PROTEIN 42 HOMOLOG (chains B)
SHMQTIKCVVVGDGAVGKTCLLISYTTNKFPSEYVPTVFDNYAVTVMIGGEPYTLGLFDT
AGQEDYDRLRPLSYPQTDVFLVCFSVVSPSSFENVKEKWVPEITHHCPKTPFLLVGTQID
LRDDPSTIEKLAKNKQKPITPETAEKLARDLKAVKYVECSALTQKGLKNVFDEAILAALE
PPEPKKSRRC

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	1

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:

2WM9 2.2 Å, Structure of the complex between DOCK9 and Cdc42.
2WMO 2.2 Å, Structure of the complex between DOCK9 and Cdc42.
1WG7 Solution structure of pleckstrin homology domain from human KIAA1058 protein

Browse structure collections

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