8r3h

Phalloidin bound F-actin

Method: ELECTRON MICROSCOPY Dmax: 172.5 Å Quality: GOOD

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

Actin, alpha skeletal muscle

Gallus

UniProt P68139

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain F; UniProt 1–377 Chain G; UniProt 1–377 Chain H; UniProt 1–377 Chain I; UniProt 1–377 Chain J; UniProt 1–377 Non-standard monomer:Yes (specific site not provided by mmCIF) phalloidin × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 3.13 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.

57 other PDB entries and 66 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain F; PDBConstruct 1–377; UniProt 1–377 Author chain G; PDBConstruct 1–377; UniProt 1–377 Author chain H; PDBConstruct 1–377; UniProt 1–377 Author chain I; PDBConstruct 1–377; UniProt 1–377 Author chain J; PDBConstruct 1–377; UniProt 1–377

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 8r3h

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8r3h
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8r3h
Deposition date deposition_date2023-11-09
Structure title titlePhalloidin bound F-actin
Keywords keywordscytoskeleton, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.67
Radius of gyration Rg (electron density) rg_electron47.27
Forward intensity I(0) i0656416000.00
Molecular weight molecular_weight209330.0 kDa
Excluded volume excluded_volume261020 ų
Envelope volume envelope_volume343740 ų
Hydration-shell volume shell_volume64535 ų
Envelope diameter envelope_diameter187.3
Shell Rg shell_rg47.16
Envelope Rg envelope_rg47.43
Shape Rg shape_rg47.28
Total Rg total_rg47.22
Total atoms total_atoms28965
Residues n_residues1847
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 dmax172.5
Rg (real space) rg_real47.23
Rg uncertainty (real space) rg_real_error2.30
I(0) (real space) i0_real6.5640e+08
I(0) uncertainty (real space) i0_real_error1.3240e+07
Rg (reciprocal space) rg_reciprocal46.68
I(0) (reciprocal space) i0_reciprocal656000000.0000
Solution quality estimate total_estimate0.8094
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.7
Skewness Skewness skewness0.631
Kurtosis Kurtosis kurtosis-0.080
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha70780000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.590; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.891; Smooth: 0.856

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)