9vef

The cryo-EM structure of human Piezo2-MDFIC complex (composite map)

Method: ELECTRON MICROSCOPY Dmax: 186.9 Å Quality: GOOD

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

Piezo-type mechanosensitive ion channel component 2,Green fluorescent protein

Aequorea victoria

UniProt P42212

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 2–238 Chain C; UniProt 2–238 Chain E; UniProt 2–238 Not recorded MyoD family inhibitor domain-containing protein × 3 (Q9P1T7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.75 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2770–3006; UniProt 2–238 Author chain C; PDBConstruct 2770–3006; UniProt 2–238 Author chain E; PDBConstruct 2770–3006; UniProt 2–238

Piezo-type mechanosensitive ion channel component 2,Green fluorescent protein

Aequorea victoria

UniProt Q9H5I5

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–2752 Chain C; UniProt 1–2752 Chain E; UniProt 1–2752 Not recorded MyoD family inhibitor domain-containing protein × 3 (Q9P1T7) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.75 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 PIEZ2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–2752; UniProt 1–2752 Author chain C; PDBConstruct 1–2752; UniProt 1–2752 Author chain E; PDBConstruct 1–2752; UniProt 1–2752

MyoD family inhibitor domain-containing protein

Homo sapiens

UniProt Q9P1T7

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 × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain B; UniProt 1–246 Chain D; UniProt 1–246 Chain F; UniProt 1–246 Not recorded Piezo-type mechanosensitive ion channel component 2,Green fluorescent protein × 3 (Q9H5I5,P42212) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.9 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.75 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MDFIC_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 22–267; UniProt 1–246 Author chain D; PDBConstruct 22–267; UniProt 1–246 Author chain F; PDBConstruct 22–267; UniProt 1–246

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 9vef

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9vef
Deposition date deposition_date2025-06-09
Structure title titleThe cryo-EM structure of human Piezo2-MDFIC complex (composite map)
Keywords keywordsPiezo2, mechanosensitive channel, MDFIC, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier67.99
Radius of gyration Rg (electron density) rg_electron67.47
Forward intensity I(0) i02919690000.00
Molecular weight molecular_weight494470.0 kDa
Excluded volume excluded_volume633720 ų
Envelope volume envelope_volume1131400 ų
Hydration-shell volume shell_volume140950 ų
Envelope diameter envelope_diameter197.7
Shell Rg shell_rg68.57
Envelope Rg envelope_rg64.32
Shape Rg shape_rg67.46
Total Rg total_rg67.49
Total atoms total_atoms34857
Residues n_residues4254
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 dmax186.9
Rg (real space) rg_real67.76
Rg uncertainty (real space) rg_real_error1.28
I(0) (real space) i0_real2.9200e+09
I(0) uncertainty (real space) i0_real_error5.8970e+07
Rg (reciprocal space) rg_reciprocal68.64
I(0) (reciprocal space) i0_reciprocal2924000000.0000
Solution quality estimate total_estimate0.8449
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary97.5
Skewness Skewness skewness-0.013
Kurtosis Kurtosis kurtosis-0.644
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha137700000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.997; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.989; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)