2RGN: P63RhoGEF complex with Galpha-q and RhoA

Crystal Structure of p63RhoGEF complex with Galpha-q and RhoA. Determined by X-ray diffraction at 3.5 Å resolution. Released 15 Jan 2008.

Method: X-ray diffraction
Resolution: 3.5 Å
Organisms: Rattus norvegicus, Mus musculus, Homo sapiens
Chains: 6
Atoms: 13,529
Mol. weight: 209.21 kDa
Ligands: GDP, MG, ALF
Released: 15 Jan 2008

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

Secondary structure: helices and β-sheets

2RGN contains 102 α-helices and 48 β-strands across 6 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, 8 β-strands

Element	Residues	Length	Sheet
β-strand	39-45	7	1
α-helix	52-63	12
α-helix	69-73	5
α-helix	76-96	21
α-helix	99-101	3
α-helix	106-114	9
α-helix	126-137	12
α-helix	139-146	8
α-helix	148-150	3
α-helix	157-162	6
α-helix	164-168	5
α-helix	176-181	6
β-strand	190-196	7	1
β-strand	199-205	7	1
α-helix	210-212	3
α-helix	215-219	5
β-strand	223-231	9	1
α-helix	232-236	5
β-strand	238	1	2
β-strand	246	1	2
α-helix	247-260	14
β-strand	268-274	7	1
α-helix	276-282	7
α-helix	302-315	14
β-strand	325-328	4	1
α-helix	334-354	21

Chain B: 23 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	151-154	4
α-helix	156-181	26
α-helix	182-186	5
α-helix	187-193	7
α-helix	200-202	3
α-helix	203-207	5
α-helix	210-216	7
α-helix	217-221	5
α-helix	222-229	8
α-helix	232-234	3
α-helix	235-241	7
α-helix	247-254	8
α-helix	257-263	7
α-helix	268-278	11
α-helix	284-287	4
α-helix	290-295	6
α-helix	298-308	11
α-helix	316-338	23
α-helix	339-341	3
β-strand	343	1	3
β-strand	355-364	10	3
β-strand	378-384	7	3
β-strand	387-393	7	3
β-strand	406-413	8	3
α-helix	414-416	3
β-strand	417-421	5	3
α-helix	423-425	3
β-strand	429-435	7	3
β-strand	441-448	8	3
α-helix	451-475	25
α-helix	478-489	12

Chain C: 10 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	5-11	7	4
α-helix	18-27	10
β-strand	42-47	6	4
β-strand	52-58	7	4
α-helix	70-72	3
β-strand	79-82	4	4
β-strand	83-85	3	5
α-helix	89-92	4
α-helix	95-99	5
α-helix	100-106	7
β-strand	112	1	4
β-strand	115-117	3	5
α-helix	120-123	4
α-helix	126-133	8
α-helix	138-140	3
α-helix	141-151	11
β-strand	157-158	2	5
α-helix	167-179	13

Chain D: 18 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	39-45	7	6
α-helix	52-63	12
α-helix	69-73	5
α-helix	76-96	21
α-helix	99-101	3
α-helix	106-114	9
α-helix	126-137	12
α-helix	139-146	8
α-helix	148-150	3
α-helix	157-161	5
α-helix	164-168	5
α-helix	176-181	6
β-strand	190-196	7	6
β-strand	199-205	7	6
α-helix	210-212	3
α-helix	215-219	5
β-strand	223-231	9	6
α-helix	232-236	5
β-strand	238	1	7
β-strand	246	1	7
α-helix	247-260	14
β-strand	268-274	7	6
α-helix	276-282	7
α-helix	302-315	14
β-strand	325-328	4	6
α-helix	334-354	21

Chain E: 23 helices, 8 β-strands

Element	Residues	Length	Sheet
α-helix	155-181	27
α-helix	182-186	5
α-helix	187-193	7
α-helix	200-202	3
α-helix	203-207	5
α-helix	210-216	7
α-helix	217-221	5
α-helix	222-229	8
α-helix	232-234	3
α-helix	235-241	7
α-helix	244-246	3
α-helix	247-254	8
α-helix	257-263	7
α-helix	268-278	11
α-helix	284-287	4
α-helix	290-295	6
α-helix	298-312	15
α-helix	316-338	23
α-helix	339-341	3
β-strand	343	1	8
β-strand	355-364	10	8
β-strand	378-384	7	8
β-strand	387-393	7	8
β-strand	406-413	8	8
α-helix	414-416	3
β-strand	417-421	5	8
α-helix	423-425	3
β-strand	429-435	7	8
β-strand	441-448	8	8
α-helix	451-475	25
α-helix	478-489	12

Chain F: 10 helices, 8 β-strands

Element	Residues	Length	Sheet
β-strand	6-11	6	9
α-helix	18-27	10
β-strand	42-44	3	9
β-strand	55-58	4	9
α-helix	70-72	3
β-strand	79-82	4	9
β-strand	83-85	3	10
α-helix	89-93	5
α-helix	95-99	5
α-helix	100-106	7
β-strand	112	1	9
β-strand	115-117	3	10
α-helix	120-123	4
α-helix	126-133	8
α-helix	138-140	3
α-helix	141-151	11
β-strand	157-158	2	10
α-helix	167-179	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine nucleotide-binding protein G(q)…	A, D	protein	353	Rattus norvegicus, Mus musculus	P10824 (AlphaFold model), P21279 (AlphaFold model)
Rho guanine nucleotide exchange factor 25	B, E	protein	354	Homo sapiens	Q86VW2 (AlphaFold model)
Transforming protein RhoA	C, F	protein	196	Homo sapiens	P61586 (AlphaFold model)

Sequence of entity 1 (A, D), FASTA

>2RGN_1 Guanine nucleotide-binding protein G(i) subunit alpha-1,Guanine nucleotide-binding protein G(q) subunit alpha (chains A, D)
MGCTLSAEDKAAVERSKMIDRNLREDGERSRRELKLLLLGTGESGKSTFIKQMRIIHGSG
YSDEDKRGFTKLVYQNIFTAMQAMIRAMDTLKIPYKYEHNKAHAQLVREVDVEKVSAFEN
PYVDAIKSLWNDPGIQECYDRRREYQLSDSTKYYLNDLDRVADPSYLPTQQDVLRVRVPT
TGIIEYPFDLQSVIFRMVDVGGQRSERRKWIHCFENVTSIMFLVALSEYDQVLVESDNEN
RMEESKALFRTIITYPWFQNSSVILFLNKKDLLEEKIMYSHLVDYFPEYDGPQRDAQAAR
EFILKMFVDLNPDSDKIIYSHFTCATDTENIRFVFAAVKDTILQLNLKEYNLV

Sequence of entity 2 (B, E), FASTA

>2RGN_2 Rho guanine nucleotide exchange factor 25 (chains B, E)
SEEEQKKKALERSMYVLSELVETEKMYVDDLGQIVEGYMATMAAQGVPESLRGRDRIVFG
NIQQIYEWHRDYFLQELQRCLKDPDWLAQLFIKHERRLHMYVVYCQNKPKSEHVVSEFGD
SYFEELRQQLGHRLQLNDLLIKPVQRIMKYQLLLKDFLKYYNRAGMDTADLEQAVEVMCF
VPKRCNDMMTLGRLRGFEGKLTAQGKLLGQDTFWVTEPEAGGLLSSRGRERRVFLFEQII
IFSEALGGGVRGGTQPGYVYKNSIKVSCLGLEGNLQGDPCRFALTSRGPEGGIQRYVLQA
ADPAISQAWIKHVAQILESQRDFLNALQSPIEYQRRESQTNSLGRPRGPGVGSP

Sequence of entity 3 (C, F), FASTA

>2RGN_3 Transforming protein RhoA (chains C, F)
GEFMAAIRKKLVIVGDGACGKTCLLIVFSKDQFPEVYVPTVFENYVADIEVDGKQVELAL
WDTAGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGN
KKDLRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRA
ALQARRGKKKSGCLVL

Ligands and cofactors

ID	Name	Formula	Copies
GDP	Guanosine-5'-diphosphate	C10 H15 N5 O11 P2	2
MG	Magnesium ion	Mg	2
ALF	Tetrafluoroaluminate ion	Al F4	2

Primary citation

Structure of Galphaq-p63RhoGEF-RhoA complex reveals a pathway for the activation of RhoA by GPCRs. Lutz, S., Shankaranarayanan, A., Coco, C. et al. Science (2007) 318:1923-1927. DOI 10.1126/science.1147554 · PubMed

Other PDB entries of the same protein (UniProt P10824 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1CIP 1.5 Å, Gi-alpha-1 subunit of guanine nucleotide-binding protein complexed with a GTP analogue
1SVS 1.5 Å, Structure of the K180P mutant of Gi alpha subunit bound to GppNHp.
4N0D 1.55 Å, Crystal structure of the K345L variant of the Gi alpha1 subunit bound to GTPgammaS
5KDO 1.9 Å, Heterotrimeric complex of the 4 alanine insertion variant of the Gi alpha1 subunit and…
1AS0 2.0 Å, GTP-gamma-S bound G42V GIA1
1GIA 2.0 Å, Structure of active conformations of GIA1 and the mechanism of GTP hydrolysis
1SVK 2.0 Å, Structure of the K180P mutant of Gi alpha subunit bound to AlF4 and GDP
4PAQ 2.0 Å, A conserved phenylalanine as relay between the 5 helix and the GDP binding region of…
4PAO 2.0 Å, A conserved phenylalanine as relay between the 5 helix and the GDP binding region of…
1FQJ 2.02 Å, Crystal structure of the heterotrimeric complex of the rgs domain of RGS9, the gamma…
6M8H 2.07 Å, Crystal Structure of the R208Q mutant of G(i) subunit alpha-1
1BH2 2.1 Å, A326S mutant of an inhibitory alpha subunit

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