4a7n

Structure of bare F-actin filaments obtained from the same sample as the Actin-Tropomyosin-Myosin Complex

Method: ELECTRON MICROSCOPY Dmax: 169.4 Å Quality: GOOD

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

F-ACTIN

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 × 5 PDB declaration: pentameric(5) 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 Chain E; UniProt 3–377 Non-standard monomer:Yes (specific site not provided by mmCIF) ADP ADENOSINE-5'-DIPHOSPHATE × 5 CA CALCIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:5MM TRIS, 100MM KCL, 2MM MGCL2, 50MM GLUTAMINE, 50MM ARGININE;pH 7.2;5MM TRIS, 100MM KCL, 2MM MGCL2, 50MM GLUTAMINE, 50MM ARGININE cryo-EM vitrification conditions:Cryogen ETHANE;VITRIFICATION 1 -- CRYOGEN- ETHANE, HUMIDITY- 90, TEMPERATURE- 101, INSTRUMENT- GATAN CRYOPLUNGE 3, METHOD- MANUAL BLOTTING FOR APPROXIMATELY 15 SECONDS, Resolution 8.90 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 Author chain E; 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 4a7n

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4a7n
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2. Structure Basics 2. Structure Basics

Entry ID entry_id4a7n
Deposition date deposition_date2011-11-14
Structure title titleStructure of bare F-actin filaments obtained from the same sample as the Actin-Tropomyosin-Myosin Complex
Keywords keywordsSTRUCTURAL PROTEIN, CYTOSKELETON, MYOSIN BINDING, ACTIN BINDING; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier47.43
Radius of gyration Rg (electron density) rg_electron47.86
Forward intensity I(0) i0676121000.00
Molecular weight molecular_weight211430.0 kDa
Excluded volume excluded_volume263330 ų
Envelope volume envelope_volume378120 ų
Hydration-shell volume shell_volume69528 ų
Envelope diameter envelope_diameter185.5
Shell Rg shell_rg48.15
Envelope Rg envelope_rg47.54
Shape Rg shape_rg47.88
Total Rg total_rg47.80
Total atoms total_atoms14810
Residues n_residues1870
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 dmax169.4
Rg (real space) rg_real47.89
Rg uncertainty (real space) rg_real_error1.83
I(0) (real space) i0_real6.7610e+08
I(0) uncertainty (real space) i0_real_error1.3370e+07
Rg (reciprocal space) rg_reciprocal47.44
I(0) (reciprocal space) i0_reciprocal675700000.0000
Solution quality estimate total_estimate0.8267
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary51.3
Skewness Skewness skewness0.587
Kurtosis Kurtosis kurtosis-0.130
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha88700000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.682; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.759

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)