2nz8

N-terminal DHPH cassette of Trio in complex with nucleotide-free Rac1

Method: X-RAY DIFFRACTION Dmax: 77.4 Å Quality: GOOD

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

ras-related C3 botulinum toxin substrate 1 isoform Rac1

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 A; UniProt 1–177 Fragment:soluble part (residues 1-177) triple functional domain protein × 1 (O75962) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6;291 K;100 mM sodium cacodylate pH 5.5 to 6.5, 14 to 18% (w/v) PEG 8000, and 300-500 mM calcium acetate, pH 6.0, VAPOR DIFFUSION, temperature 291K Resolution 2.00 Å R-free 0.249

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 1–177; UniProt 1–177

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 B; UniProt 1226–1535 Fragment:N-terminal DH/PH cassette (residues 1226-1535) ras-related C3 botulinum toxin substrate 1 isoform Rac1 × 1 (P63000) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION;pH 6;291 K;100 mM sodium cacodylate pH 5.5 to 6.5, 14 to 18% (w/v) PEG 8000, and 300-500 mM calcium acetate, pH 6.0, VAPOR DIFFUSION, temperature 291K Resolution 2.00 Å R-free 0.249

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 2
Chains and sequence ranges Author chain B; PDBConstruct 4–313; UniProt 1226–1535

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 2nz8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2nz8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id2nz8
Deposition date deposition_date2006-11-22
Structure title titleN-terminal DHPH cassette of Trio in complex with nucleotide-free Rac1
Keywords keywordsTrio; Rac1; Dbl-family GEF; Rho-family GTPase; DH/PH cassette, SIGNALING PROTEIN, CELL CYCLE; SIGNALING PROTEIN,CELL CYCLE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.57
Radius of gyration Rg (electron density) rg_electron23.46
Forward intensity I(0) i043492400.00
Molecular weight molecular_weight52120.0 kDa
Excluded volume excluded_volume65798 ų
Envelope volume envelope_volume82429 ų
Hydration-shell volume shell_volume28664 ų
Envelope diameter envelope_diameter81.4
Shell Rg shell_rg31.03
Envelope Rg envelope_rg23.76
Shape Rg shape_rg23.44
Total Rg total_rg24.43
Total atoms total_atoms3663
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 dmax77.4
Rg (real space) rg_real24.40
Rg uncertainty (real space) rg_real_error0.38
I(0) (real space) i0_real4.3490e+07
I(0) uncertainty (real space) i0_real_error4.9680e+05
Rg (reciprocal space) rg_reciprocal24.44
I(0) (reciprocal space) i0_reciprocal43490000.0000
Solution quality estimate total_estimate0.8990
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary31.9
Skewness Skewness skewness0.142
Kurtosis Kurtosis kurtosis-0.423
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha10320000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.897; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.995

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd2nz8a_
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
Domain ID domain_idd2nz8b1
Class classa — All alpha proteins
Fold Fold folda.87 — DBL homology domain (DH-domain)
Superfamily Superfamily superfamilya.87.1 — DBL homology domain (DH-domain)
Family Family familya.87.1.1 — DBL homology domain (DH-domain)
Domain ID domain_idd2nz8b2
Class classb — All beta proteins
Fold Fold foldb.55 — PH domain-like barrel
Superfamily Superfamily superfamilyb.55.1 — PH domain-like
Family Family familyb.55.1.1 — Pleckstrin-homology domain (PH domain)

CATH v4.4 (3 domains)

Domain ID domain_id2nz8A00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily300 — P-loop containing nucleotide triphosphate hydrolases
Domain ID domain_id2nz8B01
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_id2nz8B02
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)