6BCB: Transforming protein RhoA

A Complex between PH Domain of p114RhoGEF and Activated RhoA Bound to a GTP Analog. Determined by X-ray diffraction at 1.4 Å resolution. Released 13 Dec 2017.

Method: X-ray diffraction
Resolution: 1.4 Å
Organisms: Homo sapiens, Mus musculus
Chains: 2
Atoms: 3,062
Mol. weight: 38.27 kDa
Ligands: MG, GSP
Released: 13 Dec 2017

Explore 6BCB in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

6BCB contains 15 α-helices and 17 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: 4 helices, 11 β-strands

Element	Residues	Length	Sheet
α-helix	300-302	3
α-helix	304-314	11
β-strand	315	1	2
β-strand	320-322	3	3
β-strand	328-330	3	3
α-helix	331-334	4
β-strand	340-349	10	2
β-strand	355-363	9	2
β-strand	366-373	8	2
β-strand	376-379	4	2
β-strand	388-390	3	2
β-strand	395-399	5	2
β-strand	402-410	9	2
β-strand	417-422	6	2
α-helix	426-441	16

Chain F: 11 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	4-12	9	1
α-helix	18-27	10
β-strand	39-48	10	1
β-strand	51-60	10	1
α-helix	64-66	3
α-helix	70-72	3
β-strand	79-85	7	1
α-helix	89-94	6
α-helix	95-99	5
α-helix	100-106	7
β-strand	112-117	6	1
α-helix	119-121	3
α-helix	125-133	9
α-helix	138-140	3
α-helix	141-150	10
β-strand	155-158	4	1
α-helix	167-179	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Transforming protein RhoA	F	protein	185	Homo sapiens	P61586 (AlphaFold model)
Rho guanine nucleotide exchange factor 18	A	protein	146	Mus musculus	Q6P9R4 (AlphaFold model)

Sequence of entity 1 (F), FASTA

>6BCB_1 Transforming protein RhoA (chains F)
GILDMAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELA
LWDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVG
NKKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATR
AALQA

Sequence of entity 2 (A), FASTA

>6BCB_2 Rho guanine nucleotide exchange factor 18 (chains A)
AIHYEKDQRLKEIAAKTDQKSSGKLKNGLTFRKEDMLQQRQLHLEGALCWKSTSGRLKDV
LAVLLTDVLLLLQEKDQKYVFASVDSKPPVISLQKLIVREVANEEKAMFLISASMQGPEM
YEMYTSSKEDRNIWMAHIRRAVESCP

Ligands and cofactors

ID	Name	Formula	Copies
MG	Magnesium ion	Mg	1
GSP	5'-guanosine-diphosphate-monothiophosphate	C10 H16 N5 O13 P3 S	1

Water and common crystallization additives (EDO) are not listed.

Primary citation

Crystal structures of the PH domains from Lbc family of RhoGEFs bound to activated RhoA GTPase. Chen, Z., Gutowski, S., Sternweis, P.C. Data Brief (2018) 17:356-362. DOI 10.1016/j.dib.2018.01.024 · PubMed

Other PDB entries of the same protein (UniProt P61586 (AlphaFold model), which also has an AlphaFold model), best resolution first:

6V6U 1.16 Å, Crystal structure of RhoA-GDP with novel Switch I conformation
5C4M 1.3 Å, RhoA GDP with novel switch II conformation
7G83 1.31 Å, ARHGEF2 PanDDA analysis group deposition -- ARHGEF2 and RhoA in complex with Z108545814
7G8T 1.39 Å, ARHGEF2 PanDDA analysis group deposition -- ARHGEF2 and RhoA in complex with Z1273312142
6V6M 1.39 Å, Crystal structure of an inactive state of GMPPNP-bound RhoA
6V6V 1.4 Å, Crystal structure of oncogenic RhoA mutant G14V complexed with GDP
8BNT 1.4 Å, The DH domain of ARHGEF2 bound to RhoA
8FPW 1.4 Å, Crystal structure of tumor related RhoA mutant A161V in complex with GDP
8GI6 1.4 Å, Crystal structure of RhoA mutant L69R complexed with GDP
7G82 1.41 Å, ARHGEF2 PanDDA analysis group deposition -- ARHGEF2 and RhoA in complex with Z1079512010
5C2K 1.42 Å, Crystal structure of the fusion protein linked by RhoA and the GAP domain of MgcRacGAP
7G8B 1.42 Å, ARHGEF2 PanDDA analysis group deposition -- ARHGEF2 and RhoA in complex with Z100643660

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