7sj4

Human Trio residues 1284-1959 in complex with Rac1

Method: ELECTRON MICROSCOPY Dmax: 79.1 Å Quality: EXCELLENT

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

Triple functional domain protein

Homo sapiens

UniProt O75962

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 1284–1959 Not recorded Ras-related C3 botulinum toxin substrate 1 × 1 (P63000) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot force 10 Resolution 2.86 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.

3 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRIO_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–679; UniProt 1284–1959

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 1–192 Not recorded Triple functional domain protein × 1 (O75962) ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE;Blot force 10 Resolution 2.86 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.

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 4–195; UniProt 1–192

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 7sj4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7sj4
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id7sj4
Deposition date deposition_date2021-10-15
Structure title titleHuman Trio residues 1284-1959 in complex with Rac1
Keywords keywordsguanine nucleotide exchange factor, GTPase, dbl homology, pleckstrin homology, signaling protein; SIGNALING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier25.74
Radius of gyration Rg (electron density) rg_electron24.59
Forward intensity I(0) i048814500.00
Molecular weight molecular_weight55253.0 kDa
Excluded volume excluded_volume69687 ų
Envelope volume envelope_volume88755 ų
Hydration-shell volume shell_volume29754 ų
Envelope diameter envelope_diameter82.5
Shell Rg shell_rg32.14
Envelope Rg envelope_rg24.70
Shape Rg shape_rg24.58
Total Rg total_rg25.50
Total atoms total_atoms3885
Residues n_residues481
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 dmax79.1
Rg (real space) rg_real25.60
Rg uncertainty (real space) rg_real_error0.39
I(0) (real space) i0_real4.8810e+07
I(0) uncertainty (real space) i0_real_error6.8360e+05
Rg (reciprocal space) rg_reciprocal25.65
I(0) (reciprocal space) i0_reciprocal48820000.0000
Solution quality estimate total_estimate0.9093
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.1
Skewness Skewness skewness0.134
Kurtosis Kurtosis kurtosis-0.510
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10100000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.945; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.990

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7sj4A01
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_id7sj4A02
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)

8. Citations (1)

9. Files and Curves (10)