3T06: Rho guanine nucleotide exchange factor 11

Crystal Structure of the DH/PH fragment of PDZRHOGEF with N-terminal regulatory elements in complex with Human RhoA. Determined by X-ray diffraction at 2.84 Å resolution. Released 3 Aug 2011.

Method: X-ray diffraction
Resolution: 2.84 Å
Organism: Homo sapiens
Chains: 4
Atoms: 8,657
Mol. weight: 137.25 kDa
Released: 3 Aug 2011

Explore 3T06 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3T06 contains 57 α-helices and 35 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: 18 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	730-755	26
α-helix	756-762	7
α-helix	763-766	4
α-helix	772-778	7
α-helix	782-799	18
α-helix	800-802	3
α-helix	810-817	8
α-helix	820-834	15
α-helix	836-849	14
α-helix	851-860	10
α-helix	864-866	3
α-helix	871-874	4
α-helix	877-894	18
α-helix	901-938	38
β-strand	940-941	2	1
α-helix	961-963	3
α-helix	965	1
β-strand	966-974	9	2
β-strand	977	1	3
β-strand	980	1	3
β-strand	983-989	7	2
β-strand	992-996	5	2
β-strand	997-998	2	1
β-strand	1003-1004	2	1
β-strand	1025-1027	3	2
α-helix	1028-1030	3
β-strand	1031-1035	5	2
β-strand	1042-1047	6	2
β-strand	1056-1060	5	2
α-helix	1064-1079	16

Chain B: 9 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	4
α-helix	18-27	10
β-strand	42-48	7	4
β-strand	51-59	9	4
α-helix	70-73	4
β-strand	79-85	7	4
α-helix	89-94	6
α-helix	95-99	5
α-helix	100-106	7
β-strand	112-117	6	4
α-helix	119-121	3
α-helix	125-133	9
α-helix	141-150	10
β-strand	155-158	4	4
α-helix	167-179	13

Chain E: 19 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	724-727	4
α-helix	731-755	25
α-helix	756-761	6
α-helix	762-766	5
α-helix	772-778	7
α-helix	782-801	20
α-helix	810-817	8
α-helix	820-834	15
α-helix	836-849	14
α-helix	851-861	11
α-helix	864-866	3
α-helix	871-874	4
α-helix	877-894	18
α-helix	901-936	36
α-helix	937-939	3
β-strand	940	1	5
α-helix	951-954	4
α-helix	961-963	3
β-strand	966-975	10	5
β-strand	981-989	9	5
β-strand	992-998	7	5
β-strand	1003-1004	2	5
β-strand	1008	1	6
β-strand	1022	1	6
β-strand	1025-1027	3	5
α-helix	1028-1030	3
β-strand	1033-1035	3	5
β-strand	1042-1047	6	5
β-strand	1055-1060	6	5
α-helix	1064-1079	16

Chain F: 11 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	7
α-helix	18-27	10
β-strand	42-48	7	7
β-strand	51-59	9	7
α-helix	70-72	3
β-strand	79-85	7	7
α-helix	89-94	6
α-helix	95-99	5
α-helix	100-106	7
α-helix	110-111	2
β-strand	112-117	6	7
α-helix	119-121	3
α-helix	125-132	8
α-helix	138-140	3
α-helix	141-150	10
β-strand	155-158	4	7
α-helix	167-179	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Rho guanine nucleotide exchange factor 11	A, E	protein	418	Homo sapiens	O15085 (AlphaFold model)
Transforming protein RhoA	B, F	protein	178	Homo sapiens	P61586 (AlphaFold model)

Sequence of entity 1 (A, E), FASTA

>3T06_1 Rho guanine nucleotide exchange factor 11 (chains A, E)
TPKMGRRSIESPSLGFCTDTLLPHLLEDDLGQLSDLEPEPDAQNWQHTVGKDVVAGLTQR
EIDRQEVINELFVTEASHLRTLRVLDLIFYQRMKKENLMPREELARLFPNLPELIEIHNS
WCEAMKKLREEGPIIKEISDLMLARFDGPAREELQQVAAQFCSYQSIALELIKTKQRKES
RFQLFMQEAESHPQCRRLQLRDLIISEMQRLTKYPLLLESIIKHTEGGTSEHEKLCRARD
QCREILKYVNEAVKQTENRHRLEGYQKRLDATALERASNPLAAEFKSLDLTTRKMIHEGP
LTWRISKDKTLDLHVLLLEDLLVLLQKQDEKLLLKCHSKTAVGSSDSKQTFSPVLKLNAV
LIRSVATDKRAFFIICTSKLGPPQIYELVALTSSDKNTWMELLEEAVRNAHHHHHHHH

Sequence of entity 2 (B, F), FASTA

>3T06_2 Transforming protein RhoA (chains B, F)
AIRKKLVIVGDGACGKTCLLIVNSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDTAG
QEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKDLR
NDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQ

Primary citation

Insights into the Molecular Activation Mechanism of the RhoA-specific Guanine Nucleotide Exchange Factor, PDZRhoGEF. Bielnicki, J.A., Shkumatov, A.V., Derewenda, U. et al. J Biol Chem (2011) 286:35163-35175. DOI 10.1074/jbc.M111.270918 · PubMed

Other PDB entries of the same protein (UniProt O15085 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1HTJ 2.2 Å, Structure of the rgs-like domain from PDZ-rhogef
5JHH 2.3 Å, Crystal structure of the ternary complex between the human RhoA, its inhibitor and the…
5TYT 2.4 Å, Crystal Structure of the PDZ domain of RhoGEF bound to CXCR2 C-terminal peptide
1XCG 2.5 Å, Crystal Structure of Human RhoA in complex with DH/PH fragment of PDZRHOGEF
5JHG 2.5 Å, Crystal structure of the complex between the human RhoA and the DH/PH domain of human…
3KZ1 2.7 Å, Crystal Structure of the Complex of PDZ-RhoGEF DH/PH domains with GTP-gamma-S Activated…
5E6P 3.21 Å, PlexinB2 cytoplasmic region/PDZ-RhoGEF PDZ domain complex
2DLS Solution structure of the PDZ domain of human Rho guanine nucleotide exchange factor 11

Browse structure collections

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