5fr1

Double acetylated RhoGDI-alpha in complex with RhoA-GDP

Method: X-RAY DIFFRACTION Dmax: 84.0 Å Quality: GOOD

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 1–193 Not recorded RHO GDP-DISSOCIATION INHIBITOR 1 × 1 (P19803) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.5;4 M SODIUM FORMATE, 0.1 M SODIUM ACETATE PH 4.5 Resolution 2.75 Å R-free 0.256

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 165 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 4–196; UniProt 1–193

RHO GDP-DISSOCIATION INHIBITOR 1

BOS TAURUS

UniProt P19803

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 B; UniProt 1–204 Non-standard monomer:Yes (specific site not provided by mmCIF) TRANSFORMING PROTEIN RHOA × 1 (P61586) GDP GUANOSINE-5'-DIPHOSPHATE × 1 MG MAGNESIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:pH 4.5;4 M SODIUM FORMATE, 0.1 M SODIUM ACETATE PH 4.5 Resolution 2.75 Å R-free 0.256

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.

4 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GDIR1_BOVIN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 10–213; 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 5fr1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5fr1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5fr1
Deposition date deposition_date2015-12-15
Structure title titleDouble acetylated RhoGDI-alpha in complex with RhoA-GDP
Keywords keywords;SIGNALING PROTEIN, RAS-SUPERFAMILY, GUANINE-NUCLEOTIDE-BINDING PROTEIN, MOLECULAR SWITCH, ACTIN-CYTOSKELETON RHOGDI-ALPHA, NUCLEOTIDE DISSOCIATION, PRENYLATION, LYSINE-ACETYLATION ;; SIGNALING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.37
Radius of gyration Rg (electron density) rg_electron23.59
Forward intensity I(0) i028573400.00
Molecular weight molecular_weight40759.0 kDa
Excluded volume excluded_volume50985 ų
Envelope volume envelope_volume62409 ų
Hydration-shell volume shell_volume22877 ų
Envelope diameter envelope_diameter88.5
Shell Rg shell_rg29.79
Envelope Rg envelope_rg24.01
Shape Rg shape_rg23.56
Total Rg total_rg24.44
Total atoms total_atoms5690
Residues n_residues349
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 dmax84.0
Rg (real space) rg_real24.49
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real2.8570e+07
I(0) uncertainty (real space) i0_real_error3.7630e+05
Rg (reciprocal space) rg_reciprocal24.46
I(0) (reciprocal space) i0_reciprocal28570000.0000
Solution quality estimate total_estimate0.8593
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.0
Skewness Skewness skewness0.478
Kurtosis Kurtosis kurtosis-0.217
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7971000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.777; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.850; Smooth: 0.988

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd5fr1a_
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.37.1.0 — automated matches
Domain ID domain_idd5fr1b_
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

CATH v4.4 (2 domains)

Domain ID domain_id5fr1A00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id5fr1B00
Class class2 — Mainly Beta
Architecture architecture70 — Distorted Sandwich
Topology topology50 — Coagulation Factor XIII; Chain A, domain 1
Homologous superfamily homologous superfamily30 — Coagulation Factor XIII, subunit A, domain 1

8. Citations (1)

9. Files and Curves (10)