1CC0: Rhoa.gdp-rhogdi complex

Crystal structure of the rhoa.gdp-rhogdi complex. Determined by X-ray diffraction at 5.0 Å resolution. Released 7 Jan 2000.

Method: X-ray diffraction
Resolution: 5.0 Å
Organism: Homo sapiens
Chains: 4
Atoms: 5,174
Mol. weight: 90.29 kDa
Ligands: GDP, MG
Released: 7 Jan 2000

Explore 1CC0 in 3D Show helices and sheets RCSB PDB PDBe

Secondary structure: helices and β-sheets

1CC0 contains 26 α-helices and 34 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.

Chains A and C: 11 helices, 6 β-strands

Element	Residues	Length	Sheet
β-strand	5-12	8	1
α-helix	18-27	10
β-strand	43-47	5	1
β-strand	52-58	7	1
α-helix	65-67	3
α-helix	70-73	4
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	125-132	8
α-helix	138-140	3
α-helix	141-151	11
β-strand	155-158	4	1
α-helix	167-179	13

Chains E and F: 2 helices, 11 β-strands

Element	Residues	Length	Sheet
β-strand	70-78	9	2
β-strand	87-89	3	2
α-helix	95-99	5
β-strand	102-105	4	3
β-strand	109-110	2	4
β-strand	111-118	8	2
β-strand	123-134	12	3
β-strand	137-149	13	3
β-strand	156-159	4	2
α-helix	160-162	3
β-strand	163-164	2	4
β-strand	173-182	10	3
β-strand	190-199	10	3

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
transforming protein rhoA	A, C	protein	190	Homo sapiens	P61586 (AlphaFold model)
rho GDP dissociation inhibitor alpha	E, F	protein	204	Homo sapiens	P52565 (AlphaFold model)

Sequence of entity 1 (A, C), FASTA

>1CC0_1 transforming protein rhoA (chains A, C)
MAAIRKKLVIVGDGACGKTCLLIVNSKDQFPEVYVPTVFENYVADIEVDGKQVELALWDT
AGQEDYDRLRPLSYPDTDVILMCFSIDSPDSLENIPEKWTPEVKHFCPNVPIILVGNKKD
LRNDEHTRRELAKMKQEPVKPEEGRDMANRIGAFGYMECSAKTKDGVREVFEMATRAALQ
ARRGKKKSGC

Sequence of entity 2 (E, F), FASTA

>1CC0_2 rho GDP dissociation inhibitor alpha (chains E, F)
MAEQEPTAEQLAQIAAENEEDEHSVNYKPPAQKSIQEIQELDKDDESLRKYKEALLGRVA
VSADPNVPNVVVTGLTLVCSSAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNR
EIVSGMKYIQHTYRKGVKIDKTDYMVGSYGPRAEEYEFLTPVEEAPKGMLARGSYSIKSR
FTDDDKTDHLSWEWNLTIKKDWKD

Ligands and cofactors

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

Primary citation

How RhoGDI binds Rho. Longenecker, K., Read, P., Derewenda, U. et al. Acta Crystallogr D Biol Crystallogr (1999) 55:1503-1515. DOI 10.1107/S090744499900801X · 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
6BCB 1.4 Å, A Complex between PH Domain of p114RhoGEF and Activated RhoA Bound to a GTP Analog
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

Browse structure collections

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