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1av3

POTASSIUM CHANNEL BLOCKER KAPPA CONOTOXIN PVIIA FROM C. PURPURASCENS, NMR, 20 STRUCTURES

Method: SOLUTION NMR Dmax: 26.1 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Kappa-conotoxin PVIIA

OrganismNot specified

UniProt P56633

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 46–72 Non-standard monomer：Yes (specific site not provided by mmCIF) No other associated polymer SOLUTION NMR NMR measurement conditions：pH 3；298 K；Pressure 1 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 1AV3 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1KCP 3D STRUCTURE OF K-CONOTOXIN PVIIA, A NOVEL POTASSIUM CHANNEL-BLOCKING TOXIN FROM CONE SNAILS, NMR, 22 STRUCTURES Deposited 1998-01-27 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 1–27（27 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 5；288 K
Resolution not provided
2N8E Three-dimensional structure of cyclic PVIIA Deposited 2015-10-13 Different construct Different experimental conditions Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric
Chain A 46–72（27 aa） Fragment：UNP residues 46-72
Non-standard monomer：Yes (specific site not provided by mmCIF) No recorded non-water small molecule SOLUTION NMR
NMR measurement conditions pH 3.5；298 K；Pressure ambient
NMR sample composition 1 mM protein, 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 O17A_CONPU
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–27； UniProt 46–72

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 1av3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1av3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1av3
Deposition date deposition_date1997-09-24
Structure title titlePOTASSIUM CHANNEL BLOCKER KAPPA CONOTOXIN PVIIA FROM C. PURPURASCENS, NMR, 20 STRUCTURES
Keywords keywordsKAPPA-CONOTOXIN, POTASSIUM CHANNEL BLOCKER, CYSTINE KNOT; POTASSIUM CHANNEL BLOCKER
Experimental Method methodSOLUTION NMR
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier7.24 Å
Radius of gyration Rg (electron density) rg_electron7.88 Å
Forward intensity I(0) i081445900.00
Molecular weight molecular_weight65617.0 kDa
Excluded volume excluded_volume78253 ų
Envelope volume envelope_volume6272 ų
Hydration-shell volume shell_volume6164 ų
Envelope diameter envelope_diameter29.0 Å
Shell Rg shell_rg14.17 Å
Envelope Rg envelope_rg9.49 Å
Shape Rg shape_rg7.88 Å
Total Rg total_rg8.09 Å
Total atoms total_atoms8760
Residues n_residues520
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 dmax26.1 Å
Rg (real space) rg_real7.25 Å
Rg uncertainty (real space) rg_real_error0.34 Å
I(0) (real space) i0_real8.1450e+07
I(0) uncertainty (real space) i0_real_error8.7120e+05
Rg (reciprocal space) rg_reciprocal7.25 Å
I(0) (reciprocal space) i0_reciprocal81450000.0000
Solution quality estimate total_estimate0.8321
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary8.6 Å
Skewness Skewness skewness0.454
Kurtosis Kurtosis kurtosis0.110
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha7385.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.683; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.893; Smooth: 0.871
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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_idd1av3a_
Class classg — Small proteins
Fold Fold foldg.3 — Knottins (small inhibitors, toxins, lectins)
Superfamily Superfamily superfamilyg.3.6 — omega toxin-like
Family Family familyg.3.6.1 — Conotoxin
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8. Citations (2)

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9. Files and Curves (10)