9cty

Human Kv1.3-H451V with A0194009G09 nanobodies conformation 2

Method: ELECTRON MICROSCOPY Dmax: 145.4 Å Quality: GOOD

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

Potassium voltage-gated channel subfamily A member 3/mVenus fusion protein,Green fluorescent protein

Aequorea victoria

UniProt P22001

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–575 Chain B; UniProt 1–575 Chain C; UniProt 1–575 Chain D; UniProt 1–575 Not recorded A0194009G09 nanobody × 4 K POTASSIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.03 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.

15 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name KCNA3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–575; UniProt 1–575 Author chain B; PDBConstruct 1–575; UniProt 1–575 Author chain C; PDBConstruct 1–575; UniProt 1–575 Author chain D; PDBConstruct 1–575; UniProt 1–575

Potassium voltage-gated channel subfamily A member 3/mVenus fusion protein,Green fluorescent protein

Aequorea victoria

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 2–238 Chain B; UniProt 2–238 Chain C; UniProt 2–238 Chain D; UniProt 2–238 Not recorded A0194009G09 nanobody × 4 K POTASSIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.03 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 590–826; UniProt 2–238 Author chain B; PDBConstruct 590–826; UniProt 2–238 Author chain C; PDBConstruct 590–826; UniProt 2–238 Author chain D; PDBConstruct 590–826; UniProt 2–238

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 9cty

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id9cty
Deposition date deposition_date2024-07-25
Structure title titleHuman Kv1.3-H451V with A0194009G09 nanobodies conformation 2
Keywords keywordsVoltage gated potassium channel, IMMUNE SYSTEM; IMMUNE SYSTEM
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.40
Radius of gyration Rg (electron density) rg_electron43.55
Forward intensity I(0) i0621838000.00
Molecular weight molecular_weight216250.0 kDa
Excluded volume excluded_volume274980 ų
Envelope volume envelope_volume381330 ų
Hydration-shell volume shell_volume72817 ų
Envelope diameter envelope_diameter145.9
Shell Rg shell_rg48.88
Envelope Rg envelope_rg42.84
Shape Rg shape_rg43.56
Total Rg total_rg43.77
Total atoms total_atoms15280
Residues n_residues1908
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 dmax145.4
Rg (real space) rg_real44.34
Rg uncertainty (real space) rg_real_error1.23
I(0) (real space) i0_real6.2180e+08
I(0) uncertainty (real space) i0_real_error1.0860e+07
Rg (reciprocal space) rg_reciprocal44.40
I(0) (reciprocal space) i0_reciprocal621900000.0000
Solution quality estimate total_estimate0.8719
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.5
Skewness Skewness skewness0.313
Kurtosis Kurtosis kurtosis-0.319
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha41950000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.861; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.750

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)