8v3g

Cryo-EM structure of the KCa2.2 channel with inhibitor UCL 1684.

Method: ELECTRON MICROSCOPY Dmax: 133.5 Å Quality: GOOD

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

Small conductance calcium-activated potassium channel protein 2

Rattus norvegicus

UniProt P70604

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 118–478 Chain B; UniProt 118–478 Chain C; UniProt 118–478 Chain D; UniProt 118–478 Fragment:UNP residues 118-478 Calmodulin-1 × 4 (P0DP29) K POTASSIUM ION × 4 Y7Z UCL1684 × 1 CA CALCIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

17 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCNN2_RAT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–361; UniProt 118–478 Author chain B; PDBConstruct 1–361; UniProt 118–478 Author chain C; PDBConstruct 1–361; UniProt 118–478 Author chain D; PDBConstruct 1–361; UniProt 118–478

Calmodulin-1

Rattus norvegicus

UniProt P0DP29

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain E; UniProt 3–148 Chain F; UniProt 3–148 Chain G; UniProt 3–148 Chain H; UniProt 3–148 Not recorded Small conductance calcium-activated potassium channel protein 2 × 4 (P70604) K POTASSIUM ION × 4 Y7Z UCL1684 × 1 CA CALCIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.10 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.

32 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM1_RAT
Isoform
PDB entities 2
Chains and sequence ranges Author chain E; PDBConstruct 1–146; UniProt 3–148 Author chain F; PDBConstruct 1–146; UniProt 3–148 Author chain G; PDBConstruct 1–146; UniProt 3–148 Author chain H; PDBConstruct 1–146; UniProt 3–148

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 8v3g

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8v3g
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8v3g
Deposition date deposition_date2023-11-27
Structure title titleCryo-EM structure of the KCa2.2 channel with inhibitor UCL 1684.
Keywords keywordsion channel, TRANSPORT PROTEIN-INHIBITOR complex; TRANSPORT PROTEIN/INHIBITOR
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.51
Radius of gyration Rg (electron density) rg_electron43.78
Forward intensity I(0) i01503250000.00
Molecular weight molecular_weight214610.0 kDa
Excluded volume excluded_volume208470 ų
Envelope volume envelope_volume435480 ų
Hydration-shell volume shell_volume80901 ų
Envelope diameter envelope_diameter139.9
Shell Rg shell_rg51.51
Envelope Rg envelope_rg41.97
Shape Rg shape_rg43.79
Total Rg total_rg44.02
Total atoms total_atoms16193
Residues n_residues2028
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 dmax133.5
Rg (real space) rg_real44.13
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real1.5030e+09
I(0) uncertainty (real space) i0_real_error2.3970e+07
Rg (reciprocal space) rg_reciprocal44.50
I(0) (reciprocal space) i0_reciprocal1504000000.0000
Solution quality estimate total_estimate0.8958
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary61.0
Skewness Skewness skewness-0.055
Kurtosis Kurtosis kurtosis-0.562
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha64470000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.918; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.958; Smooth: 0.928

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)