3KZ1: Rho guanine nucleotide exchange factor 11

Crystal Structure of the Complex of PDZ-RhoGEF DH/PH domains with GTP-gamma-S Activated RhoA. Determined by X-ray diffraction at 2.7 Å resolution. Released 28 Apr 2010.

Method: X-ray diffraction
Resolution: 2.7 Å
Organism: Homo sapiens
Chains: 4
Atoms: 8,846
Mol. weight: 131.31 kDa
Ligands: GSP, MG
Released: 28 Apr 2010

Explore 3KZ1 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

3KZ1 contains 58 α-helices and 38 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	756-761	6
α-helix	762-767	6
α-helix	772-778	7
α-helix	782-800	19
α-helix	810-817	8
α-helix	820-833	14
α-helix	836-849	14
α-helix	851-861	11
α-helix	864-866	3
α-helix	871-875	5
α-helix	877-894	18
α-helix	901-938	38
β-strand	940-941	2	1
α-helix	943-946	4
α-helix	953-956	4
α-helix	961-963	3
β-strand	966-977	12	2
β-strand	980-989	10	2
β-strand	992-996	5	2
β-strand	997-998	2	1
β-strand	1003-1004	2	1
β-strand	1009	1	3
β-strand	1021	1	3
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	1055-1060	6	2
α-helix	1064-1081	18

Chain B: 19 helices, 12 β-strands

Element	Residues	Length	Sheet
α-helix	722-725	4
α-helix	730-755	26
α-helix	756-761	6
α-helix	762-767	6
α-helix	772-778	7
α-helix	782-801	20
α-helix	810-817	8
α-helix	819-834	16
α-helix	836-849	14
α-helix	851-862	12
α-helix	864-866	3
α-helix	871-875	5
α-helix	877-894	18
α-helix	901-939	39
β-strand	940-941	2	4
α-helix	943-946	4
α-helix	951-954	4
α-helix	961-963	3
β-strand	966-977	12	5
β-strand	980-989	10	5
β-strand	992-996	5	5
β-strand	997-998	2	4
β-strand	1003-1004	2	4
β-strand	1008	1	6
β-strand	1022	1	6
β-strand	1025-1027	3	5
α-helix	1028-1030	3
β-strand	1031-1035	5	5
β-strand	1042-1047	6	5
β-strand	1055-1060	6	5
α-helix	1064-1080	17

Chain E: 11 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	7
α-helix	18-26	9
β-strand	39-48	10	7
β-strand	51-60	10	7
α-helix	64-68	5
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
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
β-strand	160	1	8
β-strand	165	1	8
α-helix	167-179	13

Chain F: 10 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	9
α-helix	18-27	10
β-strand	40-47	8	9
β-strand	52-59	8	9
α-helix	64-66	3
α-helix	70-72	3
β-strand	79-85	7	9
α-helix	90-94	5
α-helix	95-99	5
α-helix	100-106	7
β-strand	112-117	6	9
α-helix	119-121	3
α-helix	125-132	8
α-helix	141-150	10
β-strand	155-158	4	9
α-helix	167-179	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Rho guanine nucleotide exchange factor 11	A, B	protein	383	Homo sapiens	O15085 (AlphaFold model)
Transforming protein RhoA	E, F	protein	182	Homo sapiens	P61586 (AlphaFold model)

Sequence of entity 1 (A, B), FASTA

>3KZ1_1 Rho guanine nucleotide exchange factor 11 (chains A, B)
GEPDAQNWQHTVGKDVVAGLTQREIDRQEVINELFVTEASHLRTLRVLDLIFYQRMKKEN
LMPREELARLFPNLPELIEIHNSWCEAMKKLREEGPIIKEISDLMLARFDGPAREELQQV
AAQFCSYQSIALELIKTKQRKESRFQLFMQEAESHPQCRRLQLRDLIISEMQRLTKYPLL
LESIIKHTEGGTSEHEKLCRARDQCREILKYVNEAVKQTENRHRLEGYQKRLDATALERA
SNPLAAEFKSLDLTTRKMIHEGPLTWRISKDKTLDLHVLLLEDLLVLLQKQDEKLLLKCH
SKTAVGSSDSKQTFSPVLKLNAVLIRSVATDKRAFFIICTSKLGPPQIYELVALTSSDKN
TWMELLEEAVRNATRHPHHHHHH

Sequence of entity 2 (E, F), FASTA

>3KZ1_2 Transforming protein RhoA (chains E, F)
GMAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELALWD
TAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKK
DLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAAL
QA

Ligands and cofactors

ID	Name	Formula	Copies
GSP	5'-guanosine-diphosphate-monothiophosphate	C10 H16 N5 O13 P3 S	2
MG	Magnesium ion	Mg	2

Primary citation

Activated RhoA binds to the pleckstrin homology (PH) domain of PDZ-RhoGEF, a potential site for autoregulation. Chen, Z., Medina, F., Liu, M.Y. et al. J Biol Chem (2010) 285:21070-21081. DOI 10.1074/jbc.M110.122549 · 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…
3T06 2.84 Å, Crystal Structure of the DH/PH fragment of PDZRHOGEF with N-terminal regulatory elements…
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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