9rfb

Crystal Structure of Human Rac1 in Complex with the Scaffold Protein POSH (residues 321-348)

Method: X-RAY DIFFRACTION Dmax: 84.1 Å Quality: REASONABLE

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

Ras-related C3 botulinum toxin substrate 1

Homo sapiens

UniProt P63000

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 1–177 Non-standard monomer:Yes (specific site not provided by mmCIF) E3 ubiquitin-protein ligase SH3RF1 × 1 (Q7Z6J0) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;0.05 M phosphate, 20% (w/v) PEG 8000. RAC1 6 mg/mL , GMPPNP 1mM, POSH 3 mM Resolution 1.85 Å R-free 0.226
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–177 Non-standard monomer:Yes (specific site not provided by mmCIF) E3 ubiquitin-protein ligase SH3RF1 × 1 (Q7Z6J0) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 PO4 PHOSPHATE ION × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;0.05 M phosphate, 20% (w/v) PEG 8000. RAC1 6 mg/mL , GMPPNP 1mM, POSH 3 mM Resolution 1.85 Å R-free 0.226

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.

74 other PDB entries and 101 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name RAC1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–180; UniProt 1–177 Author chain B; PDBConstruct 4–180; UniProt 1–177

E3 ubiquitin-protein ligase SH3RF1

OrganismNot specified

UniProt Q7Z6J0

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 C; UniProt 321–348 Not recorded Ras-related C3 botulinum toxin substrate 1 × 1 (P63000) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;0.05 M phosphate, 20% (w/v) PEG 8000. RAC1 6 mg/mL , GMPPNP 1mM, POSH 3 mM Resolution 1.85 Å R-free 0.226
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 321–348 Not recorded Ras-related C3 botulinum toxin substrate 1 × 1 (P63000) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 PO4 PHOSPHATE ION × 2 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;277 K;0.05 M phosphate, 20% (w/v) PEG 8000. RAC1 6 mg/mL , GMPPNP 1mM, POSH 3 mM Resolution 1.85 Å R-free 0.226

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.

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SH3R1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–28; UniProt 321–348 Author chain D; PDBConstruct 1–28; UniProt 321–348

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 9rfb

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9rfb
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9rfb
Deposition date deposition_date2025-06-04
Structure title titleCrystal Structure of Human Rac1 in Complex with the Scaffold Protein POSH (residues 321-348)
Keywords keywordsGTPase GTP/GDP-Binding Nucleotide binding, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.12
Radius of gyration Rg (electron density) rg_electron23.62
Forward intensity I(0) i034791100.00
Molecular weight molecular_weight45194.0 kDa
Excluded volume excluded_volume56492 ų
Envelope volume envelope_volume67628 ų
Hydration-shell volume shell_volume24517 ų
Envelope diameter envelope_diameter91.3
Shell Rg shell_rg29.72
Envelope Rg envelope_rg24.17
Shape Rg shape_rg23.61
Total Rg total_rg24.37
Total atoms total_atoms3159
Residues n_residues398
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 dmax84.1
Rg (real space) rg_real24.23
Rg uncertainty (real space) rg_real_error0.70
I(0) (real space) i0_real3.4790e+07
I(0) uncertainty (real space) i0_real_error5.6890e+05
Rg (reciprocal space) rg_reciprocal24.20
I(0) (reciprocal space) i0_reciprocal34790000.0000
Solution quality estimate total_estimate0.5659
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary26.3
Skewness Skewness skewness0.509
Kurtosis Kurtosis kurtosis-0.085
Angular range angular_range— – 0.3300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6801000.0000
Real-space data points n_real_points65
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.716; Stabil: 0.999; Sysdev: 0.101; Positv: 1.000; Valcen: 0.904; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)