4qj3

Structure of a fragment of human phospholipase C-beta3 delta472-559, in complex with Galphaq

Method: X-RAY DIFFRACTION Dmax: 110.9 Å Quality: REASONABLE

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

Guanine nucleotide-binding protein G(q) subunit alpha

Mus musculus

UniProt P21279

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 7–359 Fragment:UNP residues 7-359 1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3 × 1 (Q01970) GDP GUANOSINE-5'-DIPHOSPHATE × 1 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;277.15 K;100 mM BisTris, 200 mM NaCl, 5% PEG 3350, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K Resolution 3.00 Å R-free 0.240

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.

9 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GNAQ_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 27–379; UniProt 7–359

1-phosphatidylinositol 4,5-bisphosphate phosphodiesterase beta-3

Homo sapiens

UniProt Q01970

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 10–470 Chain B; UniProt 570–891 Fragment:UNP residues 10-891 Guanine nucleotide-binding protein G(q) subunit alpha × 1 (P21279) GDP GUANOSINE-5'-DIPHOSPHATE × 1 ALF TETRAFLUOROALUMINATE ION × 1 MG MAGNESIUM ION × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6;277.15 K;100 mM BisTris, 200 mM NaCl, 5% PEG 3350, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 277.15K Resolution 3.00 Å R-free 0.240

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.

12 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PLCB3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 11–471; UniProt 10–470 Author chain B; PDBConstruct 472–793; UniProt 570–891

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 4qj3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4qj3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4qj3
Deposition date deposition_date2014-06-03
Structure title titleStructure of a fragment of human phospholipase C-beta3 delta472-559, in complex with Galphaq
Keywords keywords;GTP-BINDING PROTEIN ALPHA SUBUNITS, PHOSPHOLIPASE C BETA, PH DOMAIN, EF HAND, C2 DOMAIN, TIM BARREL DOMAIN, GTP HYDROLYSIS, G-PROTEIN SIGNALING, LIPASE, CALCIUM BINDING, GTP BINDING, PHOSPHOLIPIDS, membrane, SIGNALING PROTEIN-HYDROLASE complex ;; SIGNALING PROTEIN/HYDROLASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.56
Radius of gyration Rg (electron density) rg_electron32.71
Forward intensity I(0) i0234078000.00
Molecular weight molecular_weight123940.0 kDa
Excluded volume excluded_volume155670 ų
Envelope volume envelope_volume198860 ų
Hydration-shell volume shell_volume49361 ų
Envelope diameter envelope_diameter119.8
Shell Rg shell_rg40.58
Envelope Rg envelope_rg32.70
Shape Rg shape_rg32.70
Total Rg total_rg33.34
Total atoms total_atoms8719
Residues n_residues1072
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 dmax110.9
Rg (real space) rg_real33.45
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real2.3410e+08
I(0) uncertainty (real space) i0_real_error4.0860e+06
Rg (reciprocal space) rg_reciprocal33.52
I(0) (reciprocal space) i0_reciprocal234100000.0000
Solution quality estimate total_estimate0.6792
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary40.1
Skewness Skewness skewness0.204
Kurtosis Kurtosis kurtosis-0.439
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha49160000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 0.078; Positv: 1.000; Valcen: 0.999; Smooth: 0.979

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id4qj3A01
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_id4qj3A02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology400 — GI Alpha 1, domain 2-like
Homologous superfamily homologous superfamily10 — GI Alpha 1, domain 2-like
Domain ID domain_id4qj3B01
Class class2 — Mainly Beta
Architecture architecture30 — Roll
Topology topology29 — PH-domain like
Homologous superfamily homologous superfamily240
Domain ID domain_id4qj3B02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id4qj3B03
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily190 — Phosphatidylinositol (PI) phosphodiesterase
Domain ID domain_id4qj3B04
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)