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1quz

Solution structure of the potassium channel scorpion toxin HSTX1

Method: SOLUTION NMR Dmax: 30.9 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

HSTX1 TOXIN

OrganismNot specified

UniProt P59867

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 1–34 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR NMR measurement conditions：pH 4；308 K；Pressure 1 NMR sample composition：5 MG HSTX1; TSP; HCL FOR PH NMR sample composition：5 MG HSTX1; TSP; DCL FOR PD 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.

Other PDB Difference from Current Entry 1QUZ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1WPD Evidence for domain-specific recognition of SK and Kv channels by MTX and HsTx1 scorpion toxins Deposited 2004-09-01 Different construct Different mutation/modification Different oligomeric state Different experimental conditions Assembly 1 Insufficient information Monomer；Protein × 1 PDB declaration: monomeric
Chain A 21–34（14 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR mmCIF provides none of the parsed conditions Resolution not provided
1Y2P Solution structure of Hstx3P Deposited 2004-11-23 Different mutation/modification Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–34（34 aa）
Not recorded No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3；300 K；Pressure ambient
NMR measurement conditions pH 3；296 K；Pressure ambient
NMR sample composition 2Mm hstx3P, 90% H2O, 10% D2O | 90% H2O/10% D2O
Resolution not provided

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SCK1_HETSP
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–34； UniProt 1–34

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 1quz

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1quz
Deposition date deposition_date1999-07-05
Structure title titleSolution structure of the potassium channel scorpion toxin HSTX1
Keywords keywordsSCORPION TOXIN, ALPHA BETA, MOLECULAR MODELING, POTASSIUM CHANNEL, TOXIN; TOXIN
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier8.81 Å
Radius of gyration Rg (electron density) rg_electron9.10 Å
Forward intensity I(0) i0119699000.00
Molecular weight molecular_weight76652.0 kDa
Excluded volume excluded_volume90312 ų
Envelope volume envelope_volume9385 ų
Hydration-shell volume shell_volume7808 ų
Envelope diameter envelope_diameter34.0 Å
Shell Rg shell_rg15.88 Å
Envelope Rg envelope_rg10.87 Å
Shape Rg shape_rg9.08 Å
Total Rg total_rg9.35 Å
Total atoms total_atoms10220
Residues n_residues680
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 dmax30.9 Å
Rg (real space) rg_real8.85 Å
Rg uncertainty (real space) rg_real_error0.33 Å
I(0) (real space) i0_real1.1970e+08
I(0) uncertainty (real space) i0_real_error1.2850e+06
Rg (reciprocal space) rg_reciprocal8.85 Å
I(0) (reciprocal space) i0_reciprocal119700000.0000
Solution quality estimate total_estimate0.7765
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary9.4 Å
Skewness Skewness skewness0.464
Kurtosis Kurtosis kurtosis-0.100
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha16060.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.754; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.832; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (1)

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7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1quza_
Class classk — Designed proteins
Fold Fold foldk.23 — Scorpion toxin-based designs
Superfamily Superfamily superfamilyk.23.1 — Scorpion toxin-based designs
Family Family familyk.23.1.1 — Potassium channel toxin hstx1
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8. Citations (4)

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9. Files and Curves (10)