9vmx

Human PIEZO1-E756del-MDFIC

Method: ELECTRON MICROSCOPY Dmax: 199.0 Å Quality: GOOD

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

Piezo-type mechanosensitive ion channel component 1

Homo sapiens

UniProt Q92508

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 1–2521 Chain B; UniProt 1–2521 Chain D; UniProt 1–2521 Not recorded MyoD family inhibitor domain-containing protein × 3 (Q9P1T7) D12 DODECANE × 15 L9Q (1S)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(octadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PIEZ1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–2521; UniProt 1–2521 Author chain B; PDBConstruct 1–2521; UniProt 1–2521 Author chain D; PDBConstruct 1–2521; UniProt 1–2521

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 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–246 Chain E; UniProt 1–246 Chain F; UniProt 1–246 Not recorded Piezo-type mechanosensitive ion channel component 1 × 3 (Q92508) D12 DODECANE × 15 L9Q (1S)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(octadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 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.

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 C; PDBConstruct 1–246; UniProt 1–246 Author chain E; PDBConstruct 1–246; UniProt 1–246 Author chain F; PDBConstruct 1–246; 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 9vmx

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9vmx
Deposition date deposition_date2025-06-29
Structure title titleHuman PIEZO1-E756del-MDFIC
Keywords keywordsComplex of human PIEZO1-E756del and 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_guinier70.57
Radius of gyration Rg (electron density) rg_electron70.62
Forward intensity I(0) i02390030000.00
Molecular weight molecular_weight455990.0 kDa
Excluded volume excluded_volume588420 ų
Envelope volume envelope_volume1058700 ų
Hydration-shell volume shell_volume129170 ų
Envelope diameter envelope_diameter213.4
Shell Rg shell_rg67.04
Envelope Rg envelope_rg68.37
Shape Rg shape_rg70.65
Total Rg total_rg70.41
Total atoms total_atoms32172
Residues n_residues3903
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 dmax199.0
Rg (real space) rg_real70.44
Rg uncertainty (real space) rg_real_error1.15
I(0) (real space) i0_real2.3900e+09
I(0) uncertainty (real space) i0_real_error4.2940e+07
Rg (reciprocal space) rg_reciprocal70.82
I(0) (reciprocal space) i0_reciprocal2391000000.0000
Solution quality estimate total_estimate0.8322
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary99.5
Skewness Skewness skewness0.121
Kurtosis Kurtosis kurtosis-0.484
Angular range angular_range— – 0.1100 −1
Current regularization parameter α current_alpha0.0002
Highest regularization parameter α highest_alpha86100000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.936; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.010

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)