8ru0

Structure of the undecorated barbed end of F-actin.

Method: ELECTRON MICROSCOPY Dmax: 146.3 Å Quality: GOOD

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

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 homooligomer Homooligomer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 3–377 Chain B; UniProt 3–377 Chain C; UniProt 3–377 Chain D; UniProt 3–377 Non-standard monomer:Yes (specific site not provided by mmCIF) ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 4 PO4 PHOSPHATE ION × 3 ATP ADENOSINE-5'-TRIPHOSPHATE × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.1;12 mM HEPES pH 7.1, 100 mM KCl, 2.1 mM MgCl2, 1 mM EGTA, 1 mM TCEP, 0.2 mM ATP cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE;3 seconds, force 0. Resolution 3.08 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–375; UniProt 3–377 Author chain B; PDBConstruct 1–375; UniProt 3–377 Author chain C; PDBConstruct 1–375; UniProt 3–377 Author chain D; PDBConstruct 1–375; UniProt 3–377

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 8ru0

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8ru0
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8ru0
Deposition date deposition_date2024-01-29
Structure title titleStructure of the undecorated barbed end of F-actin.
Keywords keywordsactin, actin end, barbed end, actin assembly, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier41.04
Radius of gyration Rg (electron density) rg_electron41.11
Forward intensity I(0) i0426883000.00
Molecular weight molecular_weight166490.0 kDa
Excluded volume excluded_volume207350 ų
Envelope volume envelope_volume275190 ų
Hydration-shell volume shell_volume57596 ų
Envelope diameter envelope_diameter155.7
Shell Rg shell_rg44.68
Envelope Rg envelope_rg41.16
Shape Rg shape_rg41.12
Total Rg total_rg41.24
Total atoms total_atoms11660
Residues n_residues1472
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 dmax146.3
Rg (real space) rg_real41.24
Rg uncertainty (real space) rg_real_error1.44
I(0) (real space) i0_real4.2690e+08
I(0) uncertainty (real space) i0_real_error7.8760e+06
Rg (reciprocal space) rg_reciprocal41.04
I(0) (reciprocal space) i0_reciprocal426800000.0000
Solution quality estimate total_estimate0.8467
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary46.2
Skewness Skewness skewness0.551
Kurtosis Kurtosis kurtosis0.012
Angular range angular_range— – 0.1900 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha43670000.0000
Real-space data points n_real_points39
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.731; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.976; Smooth: 0.833

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)