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8yez

Human PIEZO1

Method: ELECTRON MICROSCOPY Dmax: 204.1 Å Quality: GOOD
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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 homooligomer Homooligomer Protein × 3 PDB declaration: trimeric（3） Consistent with protein copy count Chain A； UniProt 1–2521 Chain B； UniProt 1–2521 Chain C； UniProt 1–2521 Not recorded L9Q (1S)-2-{[(S)-(2-aminoethoxy)(hydroxy)phosphoryl]oxy}-1-[(octadecanoyloxy)methyl]ethyl (9Z)-octadec-9-enoate × 6 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.4 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.30 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.

Other PDB Difference from Current Entry 8YEZ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8YFC Human PIEZO1-A1988V-MDFIC Deposited 2024-02-24 Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain A 1–2521（2521 aa）
Chain B 1–2521（2521 aa）
Chain D 1–2521（2521 aa）
Not recorded 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
8YFG Human PIEZO1-R2456H_MDFIC Deposited 2024-02-24 Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain A 1–2521（2521 aa）
Chain B 1–2521（2521 aa）
Chain D 1–2521（2521 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 4.50 Å
8ZU3 Human PIEZO1-MDFIC Deposited 2024-06-07 Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain A 1–2521（2521 aa）
Chain B 1–2521（2521 aa）
Chain D 1–2521（2521 aa）
Not recorded 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 3.10 Å
8ZU8 Human PIEZO1-A1988V Deposited 2024-06-08 Different construct Different mutation/modification Different ligand/ion Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 570–2521（1952 aa）
Chain B 570–2521（1952 aa）
Chain C 570–2521（1952 aa）
Mutation：A1988V Mutation：A1988V Mutation：A1988V 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 3.90 Å
9VMX Human PIEZO1-E756del-MDFIC Deposited 2025-06-29 Different oligomeric state Different ligand/ion Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 6 PDB declaration: hexameric
Chain A 1–2521（2521 aa）
Chain B 1–2521（2521 aa）
Chain D 1–2521（2521 aa）
Not recorded 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

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 C； PDBConstruct 1–2521； UniProt 1–2521

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 8yez

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8yez
Deposition date deposition_date2024-02-23
Structure title titleHuman PIEZO1
Keywords keywordsHuman PIEZO1, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier72.82 Å
Radius of gyration Rg (electron density) rg_electron72.77 Å
Forward intensity I(0) i02277990000.00
Molecular weight molecular_weight447440.0 kDa
Excluded volume excluded_volume578060 ų
Envelope volume envelope_volume1118800 ų
Hydration-shell volume shell_volume132370 ų
Envelope diameter envelope_diameter216.8 Å
Shell Rg shell_rg69.09 Å
Envelope Rg envelope_rg70.04 Å
Shape Rg shape_rg72.76 Å
Total Rg total_rg72.71 Å
Total atoms total_atoms31599
Residues n_residues3837
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax204.1 Å
Rg (real space) rg_real72.67 Å
Rg uncertainty (real space) rg_real_error1.26 Å
I(0) (real space) i0_real2.2780e+09
I(0) uncertainty (real space) i0_real_error4.8090e+07
Rg (reciprocal space) rg_reciprocal73.16 Å
I(0) (reciprocal space) i0_reciprocal2280000000.0000
Solution quality estimate total_estimate0.8324
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary97.2 Å
Skewness Skewness skewness0.097
Kurtosis Kurtosis kurtosis-0.500
Angular range angular_range— – 0.1050 Å−1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha86180000.0000
Real-space data points n_real_points22
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.938; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.006
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (2)

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9. Files and Curves (10)