9o51

Cryo-EM structure of the human SK2-4 chimera/calmodulin channel complex in the Ca2+ free state

Method: ELECTRON MICROSCOPY Dmax: 123.8 Å Quality: GOOD

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

;Intermediate conductance calcium-activated potassium channel protein 4,Small conductance calcium-activated potassium channel protein 2 chimera ;

Homo sapiens

UniProt O15554

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–14 Chain A; UniProt 305–427 Chain B; UniProt 1–14 Chain B; UniProt 305–427 Chain C; UniProt 1–14 Chain C; UniProt 305–427 Chain D; UniProt 1–14 Chain D; UniProt 305–427 Fragment:SK4 residues 1-15 + SK2 residues 124-412 + SK4 residues 306-428 Calmodulin-1 × 4 (P0DP23) K POTASSIUM ION × 2 CA CALCIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris pH 8, 150 mM KCl, 5 mM EGTA, 0.005% GDN, 0.0005% CHS cryo-EM vitrification conditions:Cryogen ETHANE;5 uL of sample was applied to grids at 4 degree temperature with 100% humidity. After 30 seconds, grids were blotted for 5 seconds with blot force 25 and plunged into liquid ethane. Resolution 3.40 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.

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

View Construct and Data Evidence
UniProt name KCNN4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–14; UniProt 1–14 Author chain A; PDBConstruct 304–426; UniProt 305–427 Author chain B; PDBConstruct 1–14; UniProt 1–14 Author chain B; PDBConstruct 304–426; UniProt 305–427 Author chain C; PDBConstruct 1–14; UniProt 1–14 Author chain C; PDBConstruct 304–426; UniProt 305–427 Author chain D; PDBConstruct 1–14; UniProt 1–14 Author chain D; PDBConstruct 304–426; UniProt 305–427

;Intermediate conductance calcium-activated potassium channel protein 4,Small conductance calcium-activated potassium channel protein 2 chimera ;

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 Insufficient information Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 124–412 Chain B; UniProt 124–412 Chain C; UniProt 124–412 Chain D; UniProt 124–412 Fragment:SK4 residues 1-15 + SK2 residues 124-412 + SK4 residues 306-428 Calmodulin-1 × 4 (P0DP23) K POTASSIUM ION × 2 CA CALCIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris pH 8, 150 mM KCl, 5 mM EGTA, 0.005% GDN, 0.0005% CHS cryo-EM vitrification conditions:Cryogen ETHANE;5 uL of sample was applied to grids at 4 degree temperature with 100% humidity. After 30 seconds, grids were blotted for 5 seconds with blot force 25 and plunged into liquid ethane. Resolution 3.40 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 1
Chains and sequence ranges Author chain A; PDBConstruct 15–303; UniProt 124–412 Author chain B; PDBConstruct 15–303; UniProt 124–412 Author chain C; PDBConstruct 15–303; UniProt 124–412 Author chain D; PDBConstruct 15–303; UniProt 124–412

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 Insufficient information Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 1–149 Chain F; UniProt 1–149 Chain G; UniProt 1–149 Chain H; UniProt 1–149 Not recorded ;Intermediate conductance calcium-activated potassium channel protein 4,Small conductance calcium-activated potassium channel protein 2 chimera ; × 4 (O15554,Q9H2S1) K POTASSIUM ION × 2 CA CALCIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;20 mM Tris pH 8, 150 mM KCl, 5 mM EGTA, 0.005% GDN, 0.0005% CHS cryo-EM vitrification conditions:Cryogen ETHANE;5 uL of sample was applied to grids at 4 degree temperature with 100% humidity. After 30 seconds, grids were blotted for 5 seconds with blot force 25 and plunged into liquid ethane. Resolution 3.40 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 2
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 Author chain H; PDBConstruct 1–149; UniProt 1–149

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 9o51

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9o51
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9o51
Deposition date deposition_date2025-04-09
Structure title titleCryo-EM structure of the human SK2-4 chimera/calmodulin channel complex in the Ca2+ free state
Keywords keywordsIon channel, Calcium, Potassium, Calmodulin, TRANSPORT PROTEIN; TRANSPORT PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.60
Radius of gyration Rg (electron density) rg_electron40.50
Forward intensity I(0) i0427168000.00
Molecular weight molecular_weight174930.0 kDa
Excluded volume excluded_volume221550 ų
Envelope volume envelope_volume325570 ų
Hydration-shell volume shell_volume66878 ų
Envelope diameter envelope_diameter128.7
Shell Rg shell_rg46.50
Envelope Rg envelope_rg39.34
Shape Rg shape_rg40.57
Total Rg total_rg40.62
Total atoms total_atoms12302
Residues n_residues1596
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 dmax123.8
Rg (real space) rg_real41.35
Rg uncertainty (real space) rg_real_error0.85
I(0) (real space) i0_real4.2720e+08
I(0) uncertainty (real space) i0_real_error6.5330e+06
Rg (reciprocal space) rg_reciprocal41.60
I(0) (reciprocal space) i0_reciprocal427300000.0000
Solution quality estimate total_estimate0.8867
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.4
Skewness Skewness skewness0.038
Kurtosis Kurtosis kurtosis-0.472
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26010000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.926; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.974; Smooth: 0.770

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)