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1g92

SOLUTION STRUCTURE OF PONERATOXIN

Method: SOLUTION NMR Dmax: 43.6 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

PONERATOXIN

OrganismNot specified

UniProt P41736

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 1–25 Not recorded No other associated polymer SOLUTION NMR NMR measurement conditions：pH 5.5；298 K；Pressure 1 NMR sample composition：3 mM of C-amidated peptide | D2O:TFE in volumetric ratio 3:1 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 1G92 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
25IJ Cryo-EM structure of human Nav1.6 in complex with delta-paraponeritoxin-Pc1a Deposited 2026-04-06 Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 3 PDB declaration: trimeric
Chain B 1–25（25 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 4 9Z9 (3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en × 1 PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE × 3 Y01 CHOLESTEROL HEMISUCCINATE × 2 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.4
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

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

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 1g92

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1g92
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1g92
Deposition date deposition_date2000-11-22
Structure title titleSOLUTION STRUCTURE OF PONERATOXIN
Keywords keywordsToxin; Neurotoxin; Sodium channel inhibitor, 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_guinier12.12 Å
Radius of gyration Rg (electron density) rg_electron11.28 Å
Forward intensity I(0) i09192060.00
Molecular weight molecular_weight27404.0 kDa
Excluded volume excluded_volume36041 ų
Envelope volume envelope_volume16413 ų
Hydration-shell volume shell_volume10767 ų
Envelope diameter envelope_diameter45.3 Å
Shell Rg shell_rg18.73 Å
Envelope Rg envelope_rg13.53 Å
Shape Rg shape_rg11.23 Å
Total Rg total_rg12.49 Å
Total atoms total_atoms4060
Residues n_residues250
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 dmax43.6 Å
Rg (real space) rg_real12.10 Å
Rg uncertainty (real space) rg_real_error0.48 Å
I(0) (real space) i0_real9.1920e+06
I(0) uncertainty (real space) i0_real_error1.0790e+05
Rg (reciprocal space) rg_reciprocal12.10 Å
I(0) (reciprocal space) i0_reciprocal9192000.0000
Solution quality estimate total_estimate0.7598
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.0 Å
Skewness Skewness skewness0.235
Kurtosis Kurtosis kurtosis-0.051
Angular range angular_range— – 0.5000 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37530.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.645; Stabil: 0.993; Sysdev: 1.000; Positv: 1.000; Valcen: 0.960; 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_idd1g92a_
Class classj — Peptides
Fold Fold foldj.19 — Insect toxins
Superfamily Superfamily superfamilyj.19.1 — Insect toxins
Family Family familyj.19.1.2 — Poneratoxin (Pac-Tx)
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8. Citations (1)

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9. Files and Curves (10)