1cc0

CRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX

Method: X-RAY DIFFRACTION Dmax: 97.3 Å Quality: EXCELLENT

1. Protein Identity and Related Structures Protein Identity & Related Structures

transforming protein rhoA

Homo sapiens

UniProt P61586

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–190 Not recorded rho GDP dissociation inhibitor alpha × 1 (P52565) MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.3;293 K;CRYSTALS GROWN BY VAPOR DIFFUSION IN A SITTING DROP USING EQUAL VOLUMES OF PROTEIN AND RESERVOIR. CRYSTALLIZATION OCCURED OVER A PERIOD OF SEVERAL DAYS AT 20 DEGREE CELSIUS. PROTEIN (15 MG/ML) WAS IN 25MM TRIS-HCL, PH=8.0, 100MM NACL, 5MM MGCL2. RESERVOIR CONTAINED: 51% SATURATED AMMONIUM SULFATE, 100 MM SODIUM ACETATE, PH=5.3, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 5.00 Å
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–190 Not recorded rho GDP dissociation inhibitor alpha × 1 (P52565) MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.3;293 K;CRYSTALS GROWN BY VAPOR DIFFUSION IN A SITTING DROP USING EQUAL VOLUMES OF PROTEIN AND RESERVOIR. CRYSTALLIZATION OCCURED OVER A PERIOD OF SEVERAL DAYS AT 20 DEGREE CELSIUS. PROTEIN (15 MG/ML) WAS IN 25MM TRIS-HCL, PH=8.0, 100MM NACL, 5MM MGCL2. RESERVOIR CONTAINED: 51% SATURATED AMMONIUM SULFATE, 100 MM SODIUM ACETATE, PH=5.3, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 5.00 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

129 other PDB entries and 164 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RHOA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–190; UniProt 1–190 Author chain C; PDBConstruct 1–190; UniProt 1–190

rho GDP dissociation inhibitor alpha

Homo sapiens

UniProt P52565

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–204 Not recorded transforming protein rhoA × 1 (P61586) MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.3;293 K;CRYSTALS GROWN BY VAPOR DIFFUSION IN A SITTING DROP USING EQUAL VOLUMES OF PROTEIN AND RESERVOIR. CRYSTALLIZATION OCCURED OVER A PERIOD OF SEVERAL DAYS AT 20 DEGREE CELSIUS. PROTEIN (15 MG/ML) WAS IN 25MM TRIS-HCL, PH=8.0, 100MM NACL, 5MM MGCL2. RESERVOIR CONTAINED: 51% SATURATED AMMONIUM SULFATE, 100 MM SODIUM ACETATE, PH=5.3, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 5.00 Å
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 1–204 Not recorded transforming protein rhoA × 1 (P61586) MG MAGNESIUM ION × 1 GDP GUANOSINE-5'-DIPHOSPHATE × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.3;293 K;CRYSTALS GROWN BY VAPOR DIFFUSION IN A SITTING DROP USING EQUAL VOLUMES OF PROTEIN AND RESERVOIR. CRYSTALLIZATION OCCURED OVER A PERIOD OF SEVERAL DAYS AT 20 DEGREE CELSIUS. PROTEIN (15 MG/ML) WAS IN 25MM TRIS-HCL, PH=8.0, 100MM NACL, 5MM MGCL2. RESERVOIR CONTAINED: 51% SATURATED AMMONIUM SULFATE, 100 MM SODIUM ACETATE, PH=5.3, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 5.00 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

20 other PDB entries and 52 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GDIR_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–204; UniProt 1–204 Author chain F; PDBConstruct 1–204; UniProt 1–204

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 1cc0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1cc0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1cc0
Deposition date deposition_date1999-03-03
Structure title titleCRYSTAL STRUCTURE OF THE RHOA.GDP-RHOGDI COMPLEX
Keywords keywordsRHO GTPASE, G-PROTEIN, SIGNALING PROTEIN; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier31.23
Radius of gyration Rg (electron density) rg_electron30.45
Forward intensity I(0) i0114912000.00
Molecular weight molecular_weight84214.0 kDa
Excluded volume excluded_volume104790 ų
Envelope volume envelope_volume127180 ų
Hydration-shell volume shell_volume35373 ų
Envelope diameter envelope_diameter98.5
Shell Rg shell_rg37.26
Envelope Rg envelope_rg29.52
Shape Rg shape_rg29.67
Total Rg total_rg33.10
Total atoms total_atoms5066
Residues n_residues626
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax97.3
Rg (real space) rg_real31.12
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real1.1490e+08
I(0) uncertainty (real space) i0_real_error1.5430e+06
Rg (reciprocal space) rg_reciprocal31.17
I(0) (reciprocal space) i0_reciprocal114900000.0000
Solution quality estimate total_estimate0.9105
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary36.2
Skewness Skewness skewness0.158
Kurtosis Kurtosis kurtosis-0.650
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha19420000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.961; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.952

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd1cc0a_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd1cc0c_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.37 — P-loop containing nucleoside triphosphate hydrolases
Superfamily Superfamily superfamilyc.37.1 — P-loop containing nucleoside triphosphate hydrolases
Family Family familyc.37.1.8 — G proteins
Domain ID domain_idd1cc0e_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.18 — E set domains
Family Family familyb.1.18.8 — RhoGDI-like
Domain ID domain_idd1cc0f_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.18 — E set domains
Family Family familyb.1.18.8 — RhoGDI-like

8. Citations (5)

9. Files and Curves (10)