8tua

Full-length P-Rex1 in complex with inositol 1,3,4,5-tetrakisphosphate (IP4)

Method: ELECTRON MICROSCOPY Dmax: 128.0 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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 35–1659 Not recorded 4IP INOSITOL-(1,3,4,5)-TETRAKISPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.10 Å

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 1–1625; UniProt 35–1659

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 8tua

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8tua
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8tua
Deposition date deposition_date2023-08-15
最后修订 last_revision2024-04-10
Structure title titleFull-length P-Rex1 in complex with inositol 1,3,4,5-tetrakisphosphate (IP4)
Keywords keywords;Rho guanine-nucleotide exchange factor, Dbl homology domain, pleckstrin homology domain, Phosphatidylinositol 3, 4, 5-trisphosphate binding, SIGNALING PROTEIN ;; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.27
Radius of gyration Rg (electron density) rg_electron39.97
Forward intensity I(0) i0351673000.00
Molecular weight molecular_weight152320.0 kDa
Excluded volume excluded_volume190660 ų
Envelope volume envelope_volume263490 ų
Hydration-shell volume shell_volume55516 ų
Envelope diameter envelope_diameter136.0
Shell Rg shell_rg45.06
Envelope Rg envelope_rg39.26
Shape Rg shape_rg39.97
Total Rg total_rg40.26
Total atoms total_atoms21394
Residues n_residues1329
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 dmax128.0
Rg (real space) rg_real40.25
Rg uncertainty (real space) rg_real_error1.08
I(0) (real space) i0_real3.5170e+08
I(0) uncertainty (real space) i0_real_error6.1380e+06
Rg (reciprocal space) rg_reciprocal40.27
I(0) (reciprocal space) i0_reciprocal351700000.0000
Solution quality estimate total_estimate0.8928
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.2
Skewness Skewness skewness0.272
Kurtosis Kurtosis kurtosis-0.441
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36530000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.952; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.995; Smooth: 0.750

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (4)

9. Files and Curves (10)