7ajk

Crystal structure of CRYI-B Rac1 complex

Method: X-RAY DIFFRACTION Dmax: 105.9 Å Quality: GOOD

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 BBB; UniProt 2–177 Not recorded CYFIP-related Rac1 interactor B × 1 (Q9NUQ9) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;279 K;8% v/v PEG4,000 0.1M Tris pH 8.5 0.2M Sodium acetate Resolution 3.10 Å R-free 0.282

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 BBB; PDBConstruct 5–180; UniProt 2–177

CYFIP-related Rac1 interactor B

Homo sapiens

UniProt Q9NUQ9

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 CCC; UniProt 1–324 Not recorded Ras-related C3 botulinum toxin substrate 1 × 1 (P63000) MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;279 K;8% v/v PEG4,000 0.1M Tris pH 8.5 0.2M Sodium acetate Resolution 3.10 Å R-free 0.282

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name CYRIB_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain CCC; PDBConstruct 1–324; UniProt 1–324

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 7ajk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ajk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ajk
Deposition date deposition_date2020-09-29
Structure title titleCrystal structure of CRYI-B Rac1 complex
Keywords keywordsActin, cytoskeleton, Rac1, GTPase, Inhibitor, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.70
Radius of gyration Rg (electron density) rg_electron29.56
Forward intensity I(0) i043137100.00
Molecular weight molecular_weight51310.0 kDa
Excluded volume excluded_volume64369 ų
Envelope volume envelope_volume88213 ų
Hydration-shell volume shell_volume26708 ų
Envelope diameter envelope_diameter110.2
Shell Rg shell_rg34.01
Envelope Rg envelope_rg29.87
Shape Rg shape_rg29.55
Total Rg total_rg30.05
Total atoms total_atoms3600
Residues n_residues456
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 dmax105.9
Rg (real space) rg_real30.01
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real4.3140e+07
I(0) uncertainty (real space) i0_real_error6.9750e+05
Rg (reciprocal space) rg_reciprocal29.88
I(0) (reciprocal space) i0_reciprocal43130000.0000
Solution quality estimate total_estimate0.7958
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.0
Skewness Skewness skewness0.587
Kurtosis Kurtosis kurtosis-0.248
Angular range angular_range— – 0.2650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6591000.0000
Real-space data points n_real_points54
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.619; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.652; Smooth: 0.834

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)