5y7l

Solution structure of Hbeta4 extracellular loop of BK potassium channel

Method: SOLUTION NMR Dmax: 53.4 Å Quality: GOOD

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

Calcium-activated potassium channel subunit beta-4

Homo sapiens

UniProt Q86W47

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 45–166 Fragment:UNP RESIDUES 45-166 No other associated polymer SOLUTION NMR NMR measurement conditions:pH 6.8;293 K;Ionic strength (raw mmCIF value) 75;Pressure 1 NMR sample composition:0.5 mM [U-13C; U-15N] Hbeta4, 25 mM sodium phosphate, 50 mM sodium chloride, 90% H2O/10% D2O | 90% H2O/10% D2O NMR sample composition:0.5 mM [U-13C; U-15N] Hbeta4, 25 mM sodium phosphate, 50 mM sodium chloride, 100% D2O | 100% 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.

10 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCMB4_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–122; UniProt 45–166

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 5y7l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5y7l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5y7l
Deposition date deposition_date2017-08-17
Structure title titleSolution structure of Hbeta4 extracellular loop of BK potassium channel
Keywords keywordsBeta4, BK, METAL BINDING PROTEIN; METAL BINDING PROTEIN
Experimental Method methodSOLUTION NMR

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

Radius of gyration Rg (Guinier) rg_guinier15.93
Radius of gyration Rg (electron density) rg_electron15.87
Forward intensity I(0) i01300170000.00
Molecular weight molecular_weight281890.0 kDa
Excluded volume excluded_volume342180 ų
Envelope volume envelope_volume31887 ų
Hydration-shell volume shell_volume15750 ų
Envelope diameter envelope_diameter61.9
Shell Rg shell_rg23.04
Envelope Rg envelope_rg17.72
Shape Rg shape_rg15.85
Total Rg total_rg16.01
Total atoms total_atoms38020
Residues n_residues2440
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 dmax53.4
Rg (real space) rg_real15.93
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real1.3000e+09
I(0) uncertainty (real space) i0_real_error1.3920e+07
Rg (reciprocal space) rg_reciprocal15.93
I(0) (reciprocal space) i0_reciprocal1300000000.0000
Solution quality estimate total_estimate0.8852
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary18.9
Skewness Skewness skewness0.318
Kurtosis Kurtosis kurtosis-0.279
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha286200.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.856; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.968; Smooth: 0.968

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)