2fju

Activated Rac1 bound to its effector phospholipase C beta 2

Method: X-RAY DIFFRACTION Dmax: 108.8 Å Quality: GOOD

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

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 A; UniProt 1–177 Fragment:residues 1-189 1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 2 × 1 (Q00722) MG MAGNESIUM ION × 1 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;8% PEG 3350, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 2.20 Å R-free 0.226

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

1-phosphatidylinositol-4,5-bisphosphate phosphodiesterase beta 2

Homo sapiens

UniProt Q00722

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 1–799 Fragment:residues 1-799 Ras-related C3 botulinum toxin substrate 1 × 1 (P63000) MG MAGNESIUM ION × 1 GSP 5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 8.5;291 K;8% PEG 3350, pH 8.5, VAPOR DIFFUSION, SITTING DROP, temperature 291K Resolution 2.20 Å R-free 0.226

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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PLCB2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–799; UniProt 1–799

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 2fju

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id2fju
Deposition date deposition_date2006-01-03
Structure title titleActivated Rac1 bound to its effector phospholipase C beta 2
Keywords keywordsProtein-protein complex, SIGNALING PROTEIN, APOPTOSIS-HYDROLASE COMPLEX; SIGNALING PROTEIN,APOPTOSIS/HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.71
Radius of gyration Rg (electron density) rg_electron33.28
Forward intensity I(0) i0150464000.00
Molecular weight molecular_weight100080.0 kDa
Excluded volume excluded_volume126020 ų
Envelope volume envelope_volume157520 ų
Hydration-shell volume shell_volume40013 ų
Envelope diameter envelope_diameter113.3
Shell Rg shell_rg39.29
Envelope Rg envelope_rg33.46
Shape Rg shape_rg33.26
Total Rg total_rg33.81
Total atoms total_atoms7028
Residues n_residues873
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 dmax108.8
Rg (real space) rg_real33.75
Rg uncertainty (real space) rg_real_error0.96
I(0) (real space) i0_real1.5050e+08
I(0) uncertainty (real space) i0_real_error2.5810e+06
Rg (reciprocal space) rg_reciprocal33.73
I(0) (reciprocal space) i0_reciprocal150500000.0000
Solution quality estimate total_estimate0.8878
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.4
Skewness Skewness skewness0.319
Kurtosis Kurtosis kurtosis-0.574
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha35290000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.920; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.941; Smooth: 0.836

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 10 domains

SCOP 2.08 (5 domains)

Domain ID domain_idd2fjua_
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_idd2fjub1
Class classa — All alpha proteins
Fold Fold folda.39 — EF Hand-like
Superfamily Superfamily superfamilya.39.1 — EF-hand
Family Family familya.39.1.7 — EF-hand modules in multidomain proteins
Domain ID domain_idd2fjub2
Class classb — All beta proteins
Fold Fold foldb.7 — C2 domain-like
Superfamily Superfamily superfamilyb.7.1 — C2 domain (Calcium/lipid-binding domain, CaLB)
Family Family familyb.7.1.1 — PLC-like (P variant)
Domain ID domain_idd2fjub3
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)
Domain ID domain_idd2fjub4
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.18 — PLC-like phosphodiesterases
Family Family familyc.1.18.1 — Mammalian PLC

CATH v4.4 (5 domains)

Domain ID domain_id2fjuA00
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_id2fjuB01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily240
Domain ID domain_id2fjuB02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id2fjuB03
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily190 — Phosphatidylinositol (PI) phosphodiesterase
Domain ID domain_id2fjuB04
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily150 — C2 domain

8. Citations (1)

9. Files and Curves (10)