2k44

Solution structure of a K+-channel voltage-sensor paddle domain

Method: SOLUTION NMR Dmax: 30.9 Å Quality: REASONABLE

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

K+-channel voltage-sensor paddle domain of Calcium-activated potassium channel subunit alpha-1

OrganismNot specified

UniProt Q12791

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 257–284 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions:pH 5.5;310 K;Ionic strength (raw mmCIF value) 0.05;Pressure ambient NMR sample composition:100mM [U-2H] 98% DPC, 50mM potassium chloride, 1mM HsapBK(233-260), 90% H2O/10% D2O | 90% H2O/10% D2O Resolution not provided

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.

27 other PDB entries and 27 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCMA1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–28; UniProt 257–284

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 2k44

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 2k44
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id2k44
Deposition date deposition_date2008-05-28
Structure title titleSolution structure of a K+-channel voltage-sensor paddle domain
Keywords keywordspotassium channel, voltage-sensor, membrane, micelle, solution structure, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier8.84
Radius of gyration Rg (electron density) rg_electron9.35
Forward intensity I(0) i0109356000.00
Molecular weight molecular_weight101010.0 kDa
Excluded volume excluded_volume131710 ų
Envelope volume envelope_volume8427 ų
Hydration-shell volume shell_volume7112 ų
Envelope diameter envelope_diameter36.1
Shell Rg shell_rg15.75
Envelope Rg envelope_rg11.14
Shape Rg shape_rg9.32
Total Rg total_rg9.65
Total atoms total_atoms14760
Residues n_residues840
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 dmax30.9
Rg (real space) rg_real9.19
Rg uncertainty (real space) rg_real_error0.09
I(0) (real space) i0_real1.0990e+08
I(0) uncertainty (real space) i0_real_error9.0480e+05
Rg (reciprocal space) rg_reciprocal8.87
I(0) (reciprocal space) i0_reciprocal109400000.0000
Solution quality estimate total_estimate0.6667
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.274
Kurtosis Kurtosis kurtosis-0.529
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha5.0700
Highest regularization parameter α highest_alpha3046.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.907; Stabil: 0.888; Sysdev: 0.000; Positv: 1.000; Valcen: 0.661; Smooth: 0.695

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)