1QVY: RhoGDI K(199,200)R double mutant

Crystal structure of RhoGDI K(199,200)R double mutant. Determined by X-ray diffraction at 1.6 Å resolution. Released 10 Feb 2004.

Method: X-ray diffraction
Resolution: 1.6 Å
Organism: Homo sapiens
Chains: 4
Atoms: 5,291
Mol. weight: 64.87 kDa
Released: 10 Feb 2004

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

Secondary structure: helices and β-sheets

1QVY contains 16 α-helices and 48 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: 3 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	70-78	9	1
β-strand	87-89	3	1
α-helix	94-99	6
β-strand	102-105	4	2
β-strand	109-110	2	3
β-strand	111-118	8	1
β-strand	123-134	12	2
β-strand	137-149	13	2
β-strand	156-159	4	1
α-helix	160-162	3
β-strand	163-164	2	3
β-strand	167	1	4
α-helix	169-171	3
β-strand	173-182	10	2
β-strand	190-199	10	2

Chain B: 5 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	70-78	9	5
β-strand	87-89	3	5
α-helix	94-99	6
β-strand	102-105	4	6
β-strand	109-110	2	7
β-strand	111-118	8	5
β-strand	123-134	12	6
β-strand	137-149	13	6
α-helix	155	1
β-strand	156-159	4	5
α-helix	160-162	3
β-strand	163-164	2	7
α-helix	165-166	2
β-strand	167	1	4
α-helix	169-171	3
β-strand	173-183	11	6
β-strand	190-199	10	6

Chain C: 4 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	70-78	9	8
β-strand	87-89	3	8
α-helix	94-97	4
β-strand	102-105	4	9
β-strand	109-110	2	10
β-strand	111-118	8	8
β-strand	123-134	12	9
β-strand	137-149	13	9
α-helix	155	1
β-strand	156-159	4	8
α-helix	160-162	3
β-strand	163-164	2	10
β-strand	167	1	11
α-helix	169-171	3
β-strand	173-182	10	9
β-strand	190-199	10	9

Chain D: 4 helices, 12 β-strands

Element	Residues	Length	Sheet
β-strand	70-78	9	12
β-strand	87-89	3	12
α-helix	94-99	6
β-strand	102-105	4	13
β-strand	109-110	2	14
β-strand	111-118	8	12
β-strand	123-134	12	13
β-strand	137-149	13	13
α-helix	155	1
β-strand	156-159	4	12
α-helix	160-162	3
β-strand	163-164	2	14
β-strand	167	1	11
α-helix	169-171	3
β-strand	173-183	11	13
β-strand	190-199	10	13

Molecules and chains

Molecule	Chains	Type	Length	Organism	UniProt
Rho GDP-dissociation inhibitor 1	A, B, C, D	protein	139	Homo sapiens	P52565 (AlphaFold model)

Sequence of entity 1 (A, B, C, D), FASTA

>1QVY_1 Rho GDP-dissociation inhibitor 1 (chains A, B, C, D)
MVPNVVVTGLTLVCSSAPGPLELDLTGDLESFKKQSFVLKEGVEYRIKISFRVNREIVSG
MKYIQHTYRKGVKIDKTDYMVGSYGPRAEEYEFLTPVEEAPKGMLARGSYSIKSRFTDDD
KTDHLSWEWNLTIRRDWKD

Primary citation

The impact of Lys-->Arg surface mutations on the crystallization of the globular domain of RhoGDI. Czepas, J., Devedjiev, Y., Krowarsch, D. et al. Acta Crystallogr D Biol Crystallogr (2004) 60:275-280. DOI 10.1107/S0907444903026271 · PubMed

Other PDB entries of the same protein (UniProt P52565 (AlphaFold model), which also has an AlphaFold model), best resolution first:

1KMT 1.3 Å, Crystal structure of RhoGDI Glu(154,155)Ala mutant
2JHX 1.6 Å, Crystal structure of rhogdi E155H, E157H mutant
2JHU 1.65 Å, Crystal structure of rhogdi E154A,E155A mutant
2JHT 1.88 Å, Crystal structure of rhogdi K135T,K138T,K141T mutant
2JHY 1.9 Å, Crystal structure of rhogdi E155H, E157H mutant
2JHS 1.95 Å, Crystal structure of rhogdi K135H,K138H,K141H mutant
1FSO 2.0 Å, Crystal structure of truncated human rhogdi quadruple mutant
2JHV 2.07 Å, Crystal structure of rhogdi E154A,E155A mutant
2JI0 2.1 Å, Crystal structure of rhogdi K138Y, K141Y mutant
2JHZ 2.2 Å, Crystal structure of rhogdi E155S, E157S mutant
2BXW 2.4 Å, Crystal structure of rhogdi Lys(135,138,141)Tyr mutant
1RHO 2.5 Å, Structure of rho guanine nucleotide dissociation inhibitor

Browse structure collections

About this viewer

MolViewer shows 1QVY directly in your browser with nothing to install. Switch between cartoon, ball-and-stick, spacefill and surface views, color by chain, secondary structure or B-factor, measure distances, angles and dihedrals, and share or embed the view.