3eff

The Crystal Structure of Full-Length KcsA in its Closed Conformation

Method: X-RAY DIFFRACTION Dmax: 159.0 Å Quality: GOOD

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

Voltage-gated potassium channel

OrganismNot specified

UniProt P0A334

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 K; UniProt 22–160 Chain L; UniProt 22–160 Chain M; UniProt 22–160 Chain N; UniProt 22–160 Fragment:UNP residues 22-160 FAB × 2 FAB × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 5.6;298 K;340 mM (NH4)2SO4, 11% PEG4000, 100 mM Na3C6H5O7 pH 5.6, VAPOR DIFFUSION, SITTING DROP, temperature 298K Resolution 3.80 Å R-free 0.331

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.

86 other PDB entries and 96 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCSA_STRLI
Isoform
PDB entities 3
Chains and sequence ranges Author chain K; PDBConstruct 1–139; UniProt 22–160 Author chain L; PDBConstruct 1–139; UniProt 22–160 Author chain M; PDBConstruct 1–139; UniProt 22–160 Author chain N; PDBConstruct 1–139; UniProt 22–160

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 3eff

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3eff
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3eff
Deposition date deposition_date2008-09-08
Structure title titleThe Crystal Structure of Full-Length KcsA in its Closed Conformation
Keywords keywords;Full length KcsA, Bulge helix, Cell membrane, Ion transport, Ionic channel, Membrane, Transmembrane, Transport, Voltage-gated channel, MEMBRANE PROTEIN ;; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier53.54
Radius of gyration Rg (electron density) rg_electron54.67
Forward intensity I(0) i0344900000.00
Molecular weight molecular_weight154520.0 kDa
Excluded volume excluded_volume193650 ų
Envelope volume envelope_volume287150 ų
Hydration-shell volume shell_volume48201 ų
Envelope diameter envelope_diameter170.1
Shell Rg shell_rg48.51
Envelope Rg envelope_rg53.73
Shape Rg shape_rg54.62
Total Rg total_rg54.60
Total atoms total_atoms10912
Residues n_residues1424
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 dmax159.0
Rg (real space) rg_real53.68
Rg uncertainty (real space) rg_real_error1.43
I(0) (real space) i0_real3.4490e+08
I(0) uncertainty (real space) i0_real_error6.2870e+06
Rg (reciprocal space) rg_reciprocal53.38
I(0) (reciprocal space) i0_reciprocal344700000.0000
Solution quality estimate total_estimate0.8003
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary32.9
Skewness Skewness skewness0.153
Kurtosis Kurtosis kurtosis-0.970
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha12830000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.871; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.787; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 16 domains

CATH v4.4 (16 domains)

Domain ID domain_id3effA01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3effA02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3effB01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3effB02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3effC01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3effC02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3effD01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3effD02
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3effK01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily70
Domain ID domain_id3effK02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily440 — ATP synthase delta/epsilon subunit, C-terminal domain
Domain ID domain_id3effL01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily70
Domain ID domain_id3effL02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily440 — ATP synthase delta/epsilon subunit, C-terminal domain
Domain ID domain_id3effM01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily70
Domain ID domain_id3effM02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily440 — ATP synthase delta/epsilon subunit, C-terminal domain
Domain ID domain_id3effN01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology287 — Helix Hairpins
Homologous superfamily homologous superfamily70
Domain ID domain_id3effN02
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology5 — Single alpha-helices involved in coiled-coils or other helix-helix interfaces
Homologous superfamily homologous superfamily440 — ATP synthase delta/epsilon subunit, C-terminal domain

8. Citations (1)

9. Files and Curves (10)