9vu9

channel D complex with 4

Method: ELECTRON MICROSCOPY Dmax: 130.1 Å Quality: GOOD

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

Calmodulin-1

Homo sapiens

UniProt P0DP23

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain E; UniProt 1–149 Chain F; UniProt 1–149 Chain G; UniProt 1–149 Not recorded Small conductance calcium-activated potassium channel protein 2 × 4 (Q9H2S1) A1ETX (3~{S})-3-(1~{H}-benzimidazol-2-ylamino)-~{N}-(cyanomethyl)-~{N}-methyl-3-[3-(trifluoromethyl)phenyl]propanamide × 1 K POTASSIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.34 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.

213 other PDB entries and 279 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain E; PDBConstruct 1–149; UniProt 1–149 Author chain F; PDBConstruct 1–149; UniProt 1–149 Author chain G; PDBConstruct 1–149; UniProt 1–149

Small conductance calcium-activated potassium channel protein 2

Homo sapiens

UniProt Q9H2S1

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–579 Chain B; UniProt 1–579 Chain C; UniProt 1–579 Chain D; UniProt 1–579 Not recorded Calmodulin-1 × 3 (P0DP23) A1ETX (3~{S})-3-(1~{H}-benzimidazol-2-ylamino)-~{N}-(cyanomethyl)-~{N}-methyl-3-[3-(trifluoromethyl)phenyl]propanamide × 1 K POTASSIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.34 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.

15 other PDB entries and 17 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCNN2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–579; UniProt 1–579 Author chain B; PDBConstruct 1–579; UniProt 1–579 Author chain C; PDBConstruct 1–579; UniProt 1–579 Author chain D; PDBConstruct 1–579; UniProt 1–579

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 9vu9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9vu9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9vu9
Deposition date deposition_date2025-07-12
Structure title titlechannel D complex with 4
Keywords keywordschannel D complex with 4, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.96
Radius of gyration Rg (electron density) rg_electron41.23
Forward intensity I(0) i0798223000.00
Molecular weight molecular_weight156140.0 kDa
Excluded volume excluded_volume152440 ų
Envelope volume envelope_volume333820 ų
Hydration-shell volume shell_volume67197 ų
Envelope diameter envelope_diameter140.3
Shell Rg shell_rg47.13
Envelope Rg envelope_rg40.19
Shape Rg shape_rg41.24
Total Rg total_rg41.47
Total atoms total_atoms11841
Residues n_residues1551
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 dmax130.1
Rg (real space) rg_real41.74
Rg uncertainty (real space) rg_real_error0.95
I(0) (real space) i0_real7.9820e+08
I(0) uncertainty (real space) i0_real_error1.4480e+07
Rg (reciprocal space) rg_reciprocal41.96
I(0) (reciprocal space) i0_reciprocal798400000.0000
Solution quality estimate total_estimate0.8930
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary54.8
Skewness Skewness skewness0.088
Kurtosis Kurtosis kurtosis-0.474
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha36730000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.902; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.973; Smooth: 0.924

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)