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1zsx

Crystal Structure Of Human Potassium Channel Kv Beta-subunit (KCNAB2)

Method: X-RAY DIFFRACTION Dmax: 63.2 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Voltage-gated potassium channel beta-2 subunit

Homo sapiens

UniProt Q13303

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 25–346 Not recorded CL CHLORIDE ION × 16 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.2；293 K；PEG300, sodium/potassium phosphate, sodium chloride, pH 6.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.90 Å R-free 0.172
2 Protein homooligomer Homooligomer Protein × 8 PDB declaration: octameric（8） Consistent with protein copy count Chain A； UniProt 25–346 Not recorded CL CHLORIDE ION × 32 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 8 X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, SITTING DROP；pH 6.2；293 K；PEG300, sodium/potassium phosphate, sodium chloride, pH 6.2, VAPOR DIFFUSION, SITTING DROP, temperature 293K Resolution 1.90 Å R-free 0.172

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.

Other PDB Difference from Current Entry 1ZSX Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7EJ1 human voltage-gated potassium channel KV1.3 Deposited 2021-04-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 1–367（367 aa）
Chain C 1–367（367 aa）
Chain E 1–367（367 aa）
Chain G 1–367（367 aa）
Not recorded NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
7EJ2 human voltage-gated potassium channel KV1.3 H451N mutant Deposited 2021-04-01 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric
Chain A 1–367（367 aa）
Chain C 1–367（367 aa）
Chain E 1–367（367 aa）
Chain G 1–367（367 aa）
Not recorded NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.30 Å
7WF3 Composite map of human Kv1.3 channel in apo state with beta subunits Deposited 2021-12-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain C 34–361（328 aa）
Chain G 34–361（328 aa）
Chain I 34–361（328 aa）
Chain M 34–361（328 aa）
Not recorded K POTASSIUM ION × 4 NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å
7WF4 Composite map of human Kv1.3 channel in dalazatide-bound state with beta subunits Deposited 2021-12-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 12 PDB declaration: dodecameric
Chain G 34–361（328 aa）
Chain I 34–361（328 aa）
Chain M 34–361（328 aa）
Chain o 34–361（328 aa）
Not recorded NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 4 K POTASSIUM ION × 3 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.40 Å

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

View Construct and Data Evidence
UniProt name KCAB2_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 26–347； UniProt 25–346

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 1zsx

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1zsx
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1zsx
Deposition date deposition_date2005-05-25
Structure title titleCrystal Structure Of Human Potassium Channel Kv Beta-subunit (KCNAB2)
Keywords keywords;Potassium Channel, Kv Beta-subunit, human, aldo-keto reductase, Structural Genomics, SGC, Structural Genomics Consortium, OXIDOREDUCTASE ;; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier20.23 Å
Radius of gyration Rg (electron density) rg_electron19.19 Å
Forward intensity I(0) i022675600.00
Molecular weight molecular_weight36237.0 kDa
Excluded volume excluded_volume45267 ų
Envelope volume envelope_volume50582 ų
Hydration-shell volume shell_volume21524 ų
Envelope diameter envelope_diameter64.4 Å
Shell Rg shell_rg26.00 Å
Envelope Rg envelope_rg19.51 Å
Shape Rg shape_rg19.18 Å
Total Rg total_rg20.07 Å
Total atoms total_atoms2537
Residues n_residues322
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax63.2 Å
Rg (real space) rg_real20.13 Å
Rg uncertainty (real space) rg_real_error0.32 Å
I(0) (real space) i0_real2.2680e+07
I(0) uncertainty (real space) i0_real_error2.4860e+05
Rg (reciprocal space) rg_reciprocal20.15 Å
I(0) (reciprocal space) i0_reciprocal22680000.0000
Solution quality estimate total_estimate0.9013
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.3 Å
Skewness Skewness skewness0.187
Kurtosis Kurtosis kurtosis-0.451
Angular range angular_range— – 0.3950 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha6958000.0000
Real-space data points n_real_points71
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.910; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.993
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (4)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1zsxa1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.1 — TIM beta/alpha-barrel
Superfamily Superfamily superfamilyc.1.7 — NAD(P)-linked oxidoreductase
Family Family familyc.1.7.1 — Aldo-keto reductases (NADP)
Domain ID domain_idd1zsxa2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (1 domains)

Domain ID domain_id1zsxA00
Class class3 — Alpha Beta
Architecture architecture20 — Alpha-Beta Barrel
Topology topology20 — TIM Barrel
Homologous superfamily homologous superfamily100 — NADP-dependent oxidoreductase domain
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8. Citations (1)

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9. Files and Curves (10)