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9zis

C. elegans PEZO-1 Isoform G

Method: ELECTRON MICROSCOPY Dmax: 186.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Piezo-type mechanosensitive ion channel component 1

Caenorhabditis elegans

UniProt A0A061ACU2

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 1–2442 Chain B； UniProt 1–2442 Chain C； UniProt 1–2442 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.50 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 9ZIS Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
9UOX Structure of C. elegans piezo channel isoform k Deposited 2025-04-27 Different construct Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 1–1686（1686 aa）
Chain B 1–1686（1686 aa）
Chain C 1–1686（1686 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.80 Å
9UOY Structure of C. elegans piezo channel Deposited 2025-04-27 Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 1–2442（2442 aa）
Chain B 1–2442（2442 aa）
Chain C 1–2442（2442 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
9ZIT C. elegans PEZO-1 Isoform K Deposited 2025-12-04 Different construct Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 3 PDB declaration: trimeric
Chain A 757–2442（1686 aa）
Chain B 757–2442（1686 aa）
Chain C 757–2442（1686 aa）
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å

3 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PIEZ1_CAEEL
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–2442； UniProt 1–2442 Author chain B； PDBConstruct 1–2442； UniProt 1–2442 Author chain C； PDBConstruct 1–2442； UniProt 1–2442

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 9zis

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9zis
Deposition date deposition_date2025-12-04
Structure title titleC. elegans PEZO-1 Isoform G
Keywords keywordsPEZO-1, Piezo, MEMBRANE PROTEIN, mechanosensation; 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_guinier70.30 Å
Radius of gyration Rg (electron density) rg_electron69.46 Å
Forward intensity I(0) i04980910000.00
Molecular weight molecular_weight629340.0 kDa
Excluded volume excluded_volume799380 ų
Envelope volume envelope_volume1698000 ų
Hydration-shell volume shell_volume198180 ų
Envelope diameter envelope_diameter209.1 Å
Shell Rg shell_rg76.04 Å
Envelope Rg envelope_rg65.51 Å
Shape Rg shape_rg69.55 Å
Total Rg total_rg69.25 Å
Total atoms total_atoms44505
Residues n_residues5832
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 dmax186.2 Å
Rg (real space) rg_real69.99 Å
Rg uncertainty (real space) rg_real_error0.69 Å
I(0) (real space) i0_real4.9800e+09
I(0) uncertainty (real space) i0_real_error9.2640e+07
Rg (reciprocal space) rg_reciprocal71.23 Å
I(0) (reciprocal space) i0_reciprocal4992000000.0000
Solution quality estimate total_estimate0.8397
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary93.1 Å
Skewness Skewness skewness0.059
Kurtosis Kurtosis kurtosis-0.437
Angular range angular_range— – 0.1100 Å−1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha432300000.0000
Real-space data points n_real_points23
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.973; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.992; Smooth: 0.001
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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8. Citations (1)

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9. Files and Curves (10)