2wkq

Structure of a photoactivatable Rac1 containing the Lov2 C450A Mutant

Method: X-RAY DIFFRACTION Dmax: 83.2 Å Quality: GOOD

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

NPH1-1, RAS-RELATED C3 BOTULINUM TOXIN SUBSTRATE 1

HOMO SAPIENS

UniProt O49003

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 404–546 Fragment:NPH1-1 RESIDUES 404-546 AND P21-RAC1, RESIDUES 4-180 Mutation:YES GTP GUANOSINE-5'-TRIPHOSPHATE × 1 FMN FLAVIN MONONUCLEOTIDE × 1 MG MAGNESIUM ION × 1 CL CHLORIDE ION × 3 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:100 MM POTASSIUM CHLORIDE, 5% (W/V) PEG 4000 Resolution 1.60 Å R-free 0.186

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.

17 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name O49003_AVESA
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 13–155; UniProt 404–546

NPH1-1, 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 Insufficient information Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 4–180 Fragment:NPH1-1 RESIDUES 404-546 AND P21-RAC1, RESIDUES 4-180 Mutation:YES GTP GUANOSINE-5'-TRIPHOSPHATE × 1 FMN FLAVIN MONONUCLEOTIDE × 1 MG MAGNESIUM ION × 1 CL CHLORIDE ION × 3 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION X-ray crystallization conditions:100 MM POTASSIUM CHLORIDE, 5% (W/V) PEG 4000 Resolution 1.60 Å R-free 0.186

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 156–332; UniProt 4–180

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 2wkq

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2wkq
Deposition date deposition_date2009-06-16
Structure title titleStructure of a photoactivatable Rac1 containing the Lov2 C450A Mutant
Keywords keywords;TRANSFERASE, CELL ADHESION, NUCLEOTIDE-BINDING, PROTEIN ENGINEERING, RAS SUPERFAMILY LOV2, PHOTOTROPIN1, PROTEIN DESIGN, SMALL G-PROTEIN, LIGHT- INDUCED SIGNAL TRANSDUCTION, LOV2, GTPASE, RHO FAMILY, ATP-BINDING, CHIMERA, NUCLEOTIDE-BINDING PROTEIN ENGINEERING, LIGHT-INDUCED SIGNAL TRANSDUCTION, ALTERNATIVE SPLICING, CELL MEMBRANE, ADP-RIBOSYLATION, LIPOPROTEIN, GTP-BINDING ;; TRANSFERASE, CELL ADHESION
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier22.52
Radius of gyration Rg (electron density) rg_electron21.78
Forward intensity I(0) i023725000.00
Molecular weight molecular_weight36967.0 kDa
Excluded volume excluded_volume46198 ų
Envelope volume envelope_volume54376 ų
Hydration-shell volume shell_volume21524 ų
Envelope diameter envelope_diameter85.2
Shell Rg shell_rg27.97
Envelope Rg envelope_rg22.28
Shape Rg shape_rg21.76
Total Rg total_rg22.66
Total atoms total_atoms2592
Residues n_residues317
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 dmax83.2
Rg (real space) rg_real22.60
Rg uncertainty (real space) rg_real_error0.76
I(0) (real space) i0_real2.3730e+07
I(0) uncertainty (real space) i0_real_error3.5260e+05
Rg (reciprocal space) rg_reciprocal22.58
I(0) (reciprocal space) i0_reciprocal23720000.0000
Solution quality estimate total_estimate0.8200
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary24.0
Skewness Skewness skewness0.516
Kurtosis Kurtosis kurtosis-0.045
Angular range angular_range— – 0.3550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5779000.0000
Real-space data points n_real_points67
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.604; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.871; Smooth: 0.972

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id2wkqA01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology450 — Beta-Lactamase
Homologous superfamily homologous superfamily20 — PAS domain
Domain ID domain_id2wkqA02
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)