8imz

Cryo-EM structure of mouse Piezo1-MDFIC complex (composite map)

Method: ELECTRON MICROSCOPY Dmax: 181.0 Å Quality: GOOD

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

Piezo-type mechanosensitive ion channel component 1

Mus musculus

UniProt E2JF22

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–2547 Chain B; UniProt 1–2547 Chain C; UniProt 1–2547 Not recorded MyoD family inhibitor domain-containing protein × 3 (Q8BX65) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.66 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.

13 other PDB entries and 13 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PIEZ1_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–2547; UniProt 1–2547 Author chain B; PDBConstruct 1–2547; UniProt 1–2547 Author chain C; PDBConstruct 1–2547; UniProt 1–2547

MyoD family inhibitor domain-containing protein

Mus musculus

UniProt Q8BX65

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 1–247 Chain E; UniProt 1–247 Chain F; UniProt 1–247 Not recorded Piezo-type mechanosensitive ion channel component 1 × 3 (E2JF22) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.66 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name MDFIC_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–247; UniProt 1–247 Author chain E; PDBConstruct 1–247; UniProt 1–247 Author chain F; PDBConstruct 1–247; UniProt 1–247

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 8imz

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8imz
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8imz
Deposition date deposition_date2023-03-07
Structure title titleCryo-EM structure of mouse Piezo1-MDFIC complex (composite map)
Keywords keywordsPiezo1 complex, mechanosensation, mechanotransduction, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier64.57
Radius of gyration Rg (electron density) rg_electron63.21
Forward intensity I(0) i02172420000.00
Molecular weight molecular_weight416550.0 kDa
Excluded volume excluded_volume530740 ų
Envelope volume envelope_volume948400 ų
Hydration-shell volume shell_volume123390 ų
Envelope diameter envelope_diameter196.0
Shell Rg shell_rg65.66
Envelope Rg envelope_rg62.06
Shape Rg shape_rg63.27
Total Rg total_rg63.03
Total atoms total_atoms29409
Residues n_residues3732
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 dmax181.0
Rg (real space) rg_real64.22
Rg uncertainty (real space) rg_real_error1.38
I(0) (real space) i0_real2.1720e+09
I(0) uncertainty (real space) i0_real_error4.1760e+07
Rg (reciprocal space) rg_reciprocal64.82
I(0) (reciprocal space) i0_reciprocal2175000000.0000
Solution quality estimate total_estimate0.8386
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary90.5
Skewness Skewness skewness0.044
Kurtosis Kurtosis kurtosis-0.560
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha164700000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.969; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.990; Smooth: 0.002

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)