9ug2

Severed and capped actin fragment by two G1G3 domains of gelsolin

Method: ELECTRON MICROSCOPY Dmax: 157.0 Å Quality: GOOD

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

Gelsolin

Homo sapiens

UniProt P06396

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 heterocomplex Heteromer Protein × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain A; UniProt 54–401 Chain B; UniProt 54–401 Not recorded Actin, alpha skeletal muscle × 3 Actin, alpha skeletal muscle × 4 (P68135) CA CALCIUM ION × 8 ADP ADENOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 5 PO4 PHOSPHATE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 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.

60 other PDB entries and 94 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GELS_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–348; UniProt 54–401 Author chain B; PDBConstruct 1–348; UniProt 54–401

Actin, alpha skeletal muscle

OrganismNot specified

UniProt P68135

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 heterocomplex Heteromer Protein × 9 PDB declaration: nonameric(9) Consistent with protein copy count Chain C; UniProt 7–376 Chain D; UniProt 7–376 Chain E; UniProt 7–376 Chain F; UniProt 7–376 Non-standard monomer:Yes (specific site not provided by mmCIF) Actin, alpha skeletal muscle × 3 Gelsolin × 2 (P06396) CA CALCIUM ION × 8 ADP ADENOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 5 PO4 PHOSPHATE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.89 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.

293 other PDB entries and 353 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_RABIT
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–370; UniProt 7–376 Author chain D; PDBConstruct 1–370; UniProt 7–376 Author chain E; PDBConstruct 1–370; UniProt 7–376 Author chain F; PDBConstruct 1–370; UniProt 7–376

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 9ug2

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9ug2
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9ug2
Deposition date deposition_date2025-04-11
Structure title titleSevered and capped actin fragment by two G1G3 domains of gelsolin
Keywords keywordsCytoskeleton, F-actin, Actin, Actin-binding protein, Gelsolin, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.17
Radius of gyration Rg (electron density) rg_electron45.27
Forward intensity I(0) i0872511000.00
Molecular weight molecular_weight242340.0 kDa
Excluded volume excluded_volume302310 ų
Envelope volume envelope_volume403970 ų
Hydration-shell volume shell_volume74110 ų
Envelope diameter envelope_diameter169.5
Shell Rg shell_rg49.76
Envelope Rg envelope_rg45.21
Shape Rg shape_rg45.31
Total Rg total_rg45.32
Total atoms total_atoms17011
Residues n_residues2139
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 dmax157.0
Rg (real space) rg_real45.25
Rg uncertainty (real space) rg_real_error1.71
I(0) (real space) i0_real8.7250e+08
I(0) uncertainty (real space) i0_real_error1.5250e+07
Rg (reciprocal space) rg_reciprocal45.17
I(0) (reciprocal space) i0_reciprocal872400000.0000
Solution quality estimate total_estimate0.8686
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.4
Skewness Skewness skewness0.413
Kurtosis Kurtosis kurtosis-0.208
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha94900000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.811; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.969; Smooth: 0.886

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)