9rff

Crystal Structure of Human Rac1 Fused with the Scaffold Protein POSH (residues 319-371)

Method: X-RAY DIFFRACTION Dmax: 60.0 Å Quality: GOOD

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

Ras-related C3 botulinum toxin substrate 1,E3 ubiquitin-protein ligase SH3RF1

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 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–177 Non-standard monomer:Yes (specific site not provided by mmCIF) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;0.12 M ethylene glycol, 0.1 M imidazole-MES pH 6.5, 37% (v/v) 2-methyl-2,4-pentanediol (MPD)-PEG 1000-PEG 3500 2 mg/mL Rac1-POSH Resolution 1.25 Å R-free 0.164

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 102 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

Ras-related C3 botulinum toxin substrate 1,E3 ubiquitin-protein ligase SH3RF1

Homo sapiens

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 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 319–371 Non-standard monomer:Yes (specific site not provided by mmCIF) GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 MG MAGNESIUM ION × 1 MPD (4S)-2-METHYL-2,4-PENTANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;277 K;0.12 M ethylene glycol, 0.1 M imidazole-MES pH 6.5, 37% (v/v) 2-methyl-2,4-pentanediol (MPD)-PEG 1000-PEG 3500 2 mg/mL Rac1-POSH Resolution 1.25 Å R-free 0.164

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 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SH3R1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 181–233; UniProt 319–371

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 9rff

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9rff
Deposition date deposition_date2025-06-04
Structure title titleCrystal Structure of Human Rac1 Fused with the Scaffold Protein POSH (residues 319-371)
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_guinier17.91
Radius of gyration Rg (electron density) rg_electron16.94
Forward intensity I(0) i011027800.00
Molecular weight molecular_weight24828.0 kDa
Excluded volume excluded_volume31176 ų
Envelope volume envelope_volume35072 ų
Hydration-shell volume shell_volume17228 ų
Envelope diameter envelope_diameter62.2
Shell Rg shell_rg23.31
Envelope Rg envelope_rg17.44
Shape Rg shape_rg16.92
Total Rg total_rg18.00
Total atoms total_atoms1738
Residues n_residues220
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 dmax60.0
Rg (real space) rg_real17.80
Rg uncertainty (real space) rg_real_error0.46
I(0) (real space) i0_real1.1030e+07
I(0) uncertainty (real space) i0_real_error1.3840e+05
Rg (reciprocal space) rg_reciprocal17.81
I(0) (reciprocal space) i0_reciprocal11030000.0000
Solution quality estimate total_estimate0.7916
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary23.5
Skewness Skewness skewness0.199
Kurtosis Kurtosis kurtosis-0.264
Angular range angular_range— – 0.4450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2167000.0000
Real-space data points n_real_points75
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.763; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)