6bno

Structure of bare actin filament

Method: ELECTRON MICROSCOPY Dmax: 227.6 Å Quality: REASONABLE

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–373 Chain B; UniProt 1–373 Chain C; UniProt 1–373 Chain D; UniProt 1–373 Chain E; UniProt 1–373 Chain F; UniProt 1–373 Chain G; UniProt 1–373 Chain H; UniProt 1–373 Not recorded MG MAGNESIUM ION × 8 ADP ADENOSINE-5'-DIPHOSPHATE × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;Buffer was filtered through 0.44 um filter and degassed. cryo-EM vitrification conditions:Cryogen ETHANE;Sample was applied to a glow-discharged holey carbon grid, incubated for 60 seconds and blotted for 3 seconds from the backside with filter paper. Resolution 5.50 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 1–373; UniProt 1–373 Author chain B; PDBConstruct 1–373; UniProt 1–373 Author chain C; PDBConstruct 1–373; UniProt 1–373 Author chain D; PDBConstruct 1–373; UniProt 1–373 Author chain E; PDBConstruct 1–373; UniProt 1–373 Author chain F; PDBConstruct 1–373; UniProt 1–373 Author chain G; PDBConstruct 1–373; UniProt 1–373 Author chain H; PDBConstruct 1–373; UniProt 1–373

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 6bno

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6bno
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6bno
Deposition date deposition_date2017-11-17
Structure title titleStructure of bare actin filament
Keywords keywordsCytoskeleton, Filament, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier68.63
Radius of gyration Rg (electron density) rg_electron69.84
Forward intensity I(0) i01583960000.00
Molecular weight molecular_weight329870.0 kDa
Excluded volume excluded_volume411270 ų
Envelope volume envelope_volume612350 ų
Hydration-shell volume shell_volume84335 ų
Envelope diameter envelope_diameter266.2
Shell Rg shell_rg54.38
Envelope Rg envelope_rg69.67
Shape Rg shape_rg69.85
Total Rg total_rg69.45
Total atoms total_atoms23120
Residues n_residues2936
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 dmax227.6
Rg (real space) rg_real69.09
Rg uncertainty (real space) rg_real_error2.56
I(0) (real space) i0_real1.5820e+09
I(0) uncertainty (real space) i0_real_error3.7790e+07
Rg (reciprocal space) rg_reciprocal65.77
I(0) (reciprocal space) i0_reciprocal1573000000.0000
Solution quality estimate total_estimate0.7046
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary49.5
Skewness Skewness skewness0.676
Kurtosis Kurtosis kurtosis-0.325
Angular range angular_range— – 0.1150 −1
Current regularization parameter α current_alpha0.0039
Highest regularization parameter α highest_alpha106400000.0000
Real-space data points n_real_points24
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.495; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.527; Smooth: 0.147

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (2)

9. Files and Curves (10)