9liz

Human KCNQ5-CaM in complex with PIP2

Method: ELECTRON MICROSCOPY Dmax: 125.3 Å Quality: GOOD

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

Potassium voltage-gated channel subfamily KQT member 5

Homo sapiens

UniProt Q9NR82

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 90–698 Chain B; UniProt 90–698 Chain D; UniProt 90–698 Chain G; UniProt 90–698 Not recorded Calmodulin-3 × 4 (P0DP25) PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 4 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.

4 other PDB entries and 7 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCNQ5_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–610; UniProt 90–698 Author chain B; PDBConstruct 2–610; UniProt 90–698 Author chain D; PDBConstruct 2–610; UniProt 90–698 Author chain G; PDBConstruct 2–610; UniProt 90–698

Calmodulin-3

Homo sapiens

UniProt P0DP25

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 C; UniProt 1–149 Chain E; UniProt 1–149 Chain F; UniProt 1–149 Chain H; UniProt 1–149 Not recorded Potassium voltage-gated channel subfamily KQT member 5 × 4 (Q9NR82) PIO [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate × 4 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.

22 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–149; UniProt 1–149 Author chain E; PDBConstruct 1–149; UniProt 1–149 Author chain F; 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 9liz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9liz
Deposition date deposition_date2025-01-14
Structure title titleHuman KCNQ5-CaM in complex with PIP2
Keywords keywordsvoltage-gated potassium channel, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.82
Radius of gyration Rg (electron density) rg_electron41.30
Forward intensity I(0) i0697676000.00
Molecular weight molecular_weight224370.0 kDa
Excluded volume excluded_volume283910 ų
Envelope volume envelope_volume396800 ų
Hydration-shell volume shell_volume77263 ų
Envelope diameter envelope_diameter129.7
Shell Rg shell_rg49.33
Envelope Rg envelope_rg40.41
Shape Rg shape_rg41.28
Total Rg total_rg41.77
Total atoms total_atoms31648
Residues n_residues1952
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 dmax125.3
Rg (real space) rg_real41.54
Rg uncertainty (real space) rg_real_error0.90
I(0) (real space) i0_real6.9770e+08
I(0) uncertainty (real space) i0_real_error1.0970e+07
Rg (reciprocal space) rg_reciprocal41.81
I(0) (reciprocal space) i0_reciprocal697900000.0000
Solution quality estimate total_estimate0.8963
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.7
Skewness Skewness skewness0.036
Kurtosis Kurtosis kurtosis-0.497
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha51810000.0000
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: 0.961; Smooth: 0.909

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)