4yon

P-Rex1:Rac1 complex

Method: X-RAY DIFFRACTION Dmax: 97.6 Å Quality: GOOD

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

Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein

Homo sapiens

UniProt Q8TCU6

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 1–404 Fragment:UNP residues 1-404 Ras-related C3 botulinum toxin substrate 1 × 1 (P63000) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;0.1 sodium MES, pH 6.5, 0.2M sodium acetate, 15% (w/v) PEG 8000 Resolution 1.95 Å R-free 0.183

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.

12 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PREX1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–405; UniProt 1–404

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 B; UniProt 1–177 Fragment:UNP residues 1-177 Mutation:G12V Phosphatidylinositol 3,4,5-trisphosphate-dependent Rac exchanger 1 protein × 1 (Q8TCU6) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.5;293 K;0.1 sodium MES, pH 6.5, 0.2M sodium acetate, 15% (w/v) PEG 8000 Resolution 1.95 Å R-free 0.183

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 2
Chains and sequence ranges Author chain B; PDBConstruct 3–179; UniProt 1–177

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 4yon

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4yon
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4yon
Deposition date deposition_date2015-03-11
Structure title titleP-Rex1:Rac1 complex
Keywords keywordsProtein binding; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.37
Radius of gyration Rg (electron density) rg_electron28.60
Forward intensity I(0) i056803300.00
Molecular weight molecular_weight59724.0 kDa
Excluded volume excluded_volume75288 ų
Envelope volume envelope_volume97531 ų
Hydration-shell volume shell_volume29640 ų
Envelope diameter envelope_diameter102.9
Shell Rg shell_rg34.20
Envelope Rg envelope_rg28.60
Shape Rg shape_rg28.60
Total Rg total_rg29.18
Total atoms total_atoms4197
Residues n_residues525
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 dmax97.6
Rg (real space) rg_real29.43
Rg uncertainty (real space) rg_real_error0.74
I(0) (real space) i0_real5.6800e+07
I(0) uncertainty (real space) i0_real_error8.6350e+05
Rg (reciprocal space) rg_reciprocal29.41
I(0) (reciprocal space) i0_reciprocal56800000.0000
Solution quality estimate total_estimate0.8940
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary30.7
Skewness Skewness skewness0.368
Kurtosis Kurtosis kurtosis-0.397
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8337000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.898; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.957

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4yonb_
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

CATH v4.4 (3 domains)

Domain ID domain_id4yonA01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology900 — Dbl Homology Domain; Chain A
Homologous superfamily homologous superfamily10 — Dbl homology (DH) domain
Domain ID domain_id4yonA02
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily30 — Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
Domain ID domain_id4yonB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases

8. Citations (1)

9. Files and Curves (10)