1ryh

Alternative Splicing of Rac1 Generates Rac1b, a Self-activating GTPase

Method: X-RAY DIFFRACTION Dmax: 82.0 Å Quality: GOOD

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

ras-related C3 botulinum toxin substrate 1 isoform Rac1b

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–201 Fragment:residues 1-201 MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.75 Å R-free 0.219
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–201 Fragment:residues 1-201 MG MAGNESIUM ION × 1 GNP PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.75 Å R-free 0.219

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 101 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 3–203; UniProt 1–201 Author chain B; PDBConstruct 3–203; UniProt 1–201

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 1ryh

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1ryh
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1ryh
Deposition date deposition_date2003-12-22
Structure title titleAlternative Splicing of Rac1 Generates Rac1b, a Self-activating GTPase
Keywords keywordsGTP binding, HYDROLASE; HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier24.28
Radius of gyration Rg (electron density) rg_electron23.94
Forward intensity I(0) i024131100.00
Molecular weight molecular_weight37570.0 kDa
Excluded volume excluded_volume47102 ų
Envelope volume envelope_volume58025 ų
Hydration-shell volume shell_volume21335 ų
Envelope diameter envelope_diameter86.3
Shell Rg shell_rg29.64
Envelope Rg envelope_rg24.33
Shape Rg shape_rg23.95
Total Rg total_rg24.66
Total atoms total_atoms2627
Residues n_residues338
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 dmax82.0
Rg (real space) rg_real24.42
Rg uncertainty (real space) rg_real_error0.54
I(0) (real space) i0_real2.4130e+07
I(0) uncertainty (real space) i0_real_error2.9740e+05
Rg (reciprocal space) rg_reciprocal24.39
I(0) (reciprocal space) i0_reciprocal24130000.0000
Solution quality estimate total_estimate0.8604
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.4
Skewness Skewness skewness0.462
Kurtosis Kurtosis kurtosis-0.401
Angular range angular_range— – 0.3250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5110000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.791; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.816; Smooth: 0.992

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1ryha_
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_idd1ryhb_
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 (2 domains)

Domain ID domain_id1ryhA00
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_id1ryhB00
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)