9ew2

High resolution structure of FZD7 in complex with miniGs protein

Method: ELECTRON MICROSCOPY Dmax: 129.9 Å Quality: REASONABLE

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

GNAS complex locus,Isoform 4 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short

Homo sapiens

UniProt P63092

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 Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 205–395 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Ggamma × 1 Nb35 × 1 Frizzled-7 × 1 (O75084) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

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.

348 other PDB entries and 356 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GNAS2_HUMAN
Isoform P63092-4
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 68–248; UniProt 205–395

GNAS complex locus,Isoform 4 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short

Homo sapiens

UniProt Q5JWD1

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 Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 6–64 Not recorded Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Ggamma × 1 Nb35 × 1 Frizzled-7 × 1 (O75084) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

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 Q5JWD1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–59; UniProt 6–64

Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1

Homo sapiens

UniProt P62873

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 Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 1–340 Not recorded GNAS complex locus,Isoform 4 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short × 1 (Q5JWD1,P63092) Ggamma × 1 Nb35 × 1 Frizzled-7 × 1 (O75084) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

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.

1260 other PDB entries and 1263 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GBB1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–340; UniProt 1–340

Frizzled-7

Homo sapiens

UniProt O75084

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 Heteromer Protein × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain R; UniProt 38–574 Not recorded GNAS complex locus,Isoform 4 of Guanine nucleotide-binding protein G(s) subunit alpha isoforms short × 1 (Q5JWD1,P63092) Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 × 1 (P62873) Ggamma × 1 Nb35 × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.20 Å

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.

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

View Construct and Data Evidence
UniProt name FZD7_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain R; PDBConstruct 38–574; UniProt 38–574

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 9ew2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ew2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ew2
Deposition date deposition_date2024-04-03
Structure title titleHigh resolution structure of FZD7 in complex with miniGs protein
Keywords keywordsGPCPR, Frizzled, FZD7, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier37.69
Radius of gyration Rg (electron density) rg_electron37.80
Forward intensity I(0) i0232978000.00
Molecular weight molecular_weight123180.0 kDa
Excluded volume excluded_volume154020 ų
Envelope volume envelope_volume200410 ų
Hydration-shell volume shell_volume46013 ų
Envelope diameter envelope_diameter140.6
Shell Rg shell_rg41.63
Envelope Rg envelope_rg37.87
Shape Rg shape_rg37.77
Total Rg total_rg38.14
Total atoms total_atoms8660
Residues n_residues1090
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 dmax129.9
Rg (real space) rg_real38.04
Rg uncertainty (real space) rg_real_error1.30
I(0) (real space) i0_real2.3300e+08
I(0) uncertainty (real space) i0_real_error4.0010e+06
Rg (reciprocal space) rg_reciprocal37.83
I(0) (reciprocal space) i0_reciprocal232900000.0000
Solution quality estimate total_estimate0.6104
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary37.1
Skewness Skewness skewness0.571
Kurtosis Kurtosis kurtosis-0.182
Angular range angular_range— – 0.2100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha47410000.0000
Real-space data points n_real_points43
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.764; Stabil: 1.000; Sysdev: 0.020; Positv: 1.000; Valcen: 0.915; Smooth: 0.666

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)