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8zix

RAT skeletal muscle F-actin

Method: ELECTRON MICROSCOPY Dmax: 192.2 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Actin, alpha skeletal muscle

OrganismNot specified

UniProt P68136

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 × 6 PDB declaration: hexameric（6） Consistent with protein copy count Chain A； UniProt 7–377 Chain B； UniProt 7–377 Chain E； UniProt 7–377 Chain F； UniProt 7–377 Chain P； UniProt 7–377 Chain R； UniProt 7–377 Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY cryo-EM buffer：pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.54 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.

Other PDB Difference from Current Entry 8ZIX Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
3U9D Crystal Structure of a chimera containing the N-terminal domain (residues 8-24) of drosophila Ciboulot and the C-terminal domain (residues 13-44) of bovine Thymosin-beta4, bound to G-actin-ATP Deposited 2011-10-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 3–377（375 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions hanging drop；pH 6.5；298 K；18% PEG3350, 0.05M NaAcetate pH4.7, 0.1M MgAcetate pH6.5, 0.32M Guanidine HCl, 0.8% Dioxane, hanging drop, temperature 298K
Resolution 2.50 Å R-free 0.240
3U9D Crystal Structure of a chimera containing the N-terminal domain (residues 8-24) of drosophila Ciboulot and the C-terminal domain (residues 13-44) of bovine Thymosin-beta4, bound to G-actin-ATP Deposited 2011-10-18 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Insufficient information Heteromer；Protein × 2 PDB declaration: dimeric
Chain C 3–377（375 aa）
Not recorded ATP ADENOSINE-5'-TRIPHOSPHATE × 1 MG MAGNESIUM ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions hanging drop；pH 6.5；298 K；18% PEG3350, 0.05M NaAcetate pH4.7, 0.1M MgAcetate pH6.5, 0.32M Guanidine HCl, 0.8% Dioxane, hanging drop, temperature 298K
Resolution 2.50 Å R-free 0.240
8ZBM RAT skeletal muscle ATM complex Deposited 2024-04-26 Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 16 PDB declaration: 16-meric
Chain E 7–377（371 aa）
Chain H 7–377（371 aa）
Chain O 7–377（371 aa）
Chain P 7–377（371 aa）
Chain Q 7–377（371 aa）
Chain R 7–377（371 aa）
Not recorded ADP ADENOSINE-5'-DIPHOSPHATE × 6 ELECTRON MICROSCOPY
cryo-EM buffer pH 8
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.32 Å

2 other PDB entries and 3 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_RAT
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–371； UniProt 7–377 Author chain B； PDBConstruct 1–371； UniProt 7–377 Author chain E； PDBConstruct 1–371； UniProt 7–377 Author chain F； PDBConstruct 1–371； UniProt 7–377 Author chain P； PDBConstruct 1–371； UniProt 7–377 Author chain R； PDBConstruct 1–371； UniProt 7–377

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 8zix

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8zix
Deposition date deposition_date2024-05-14
最后修订 last_revision2025-01-29
Structure title titleRAT skeletal muscle F-actin
Keywords keywordsprotein fibril, filament actin; PROTEIN FIBRIL
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier53.36 Å
Radius of gyration Rg (electron density) rg_electron54.15 Å
Forward intensity I(0) i0927345000.00
Molecular weight molecular_weight250480.0 kDa
Excluded volume excluded_volume312380 ų
Envelope volume envelope_volume425080 ų
Hydration-shell volume shell_volume71497 ų
Envelope diameter envelope_diameter211.4 Å
Shell Rg shell_rg49.91 Å
Envelope Rg envelope_rg54.11 Å
Shape Rg shape_rg54.16 Å
Total Rg total_rg53.99 Å
Total atoms total_atoms17556
Residues n_residues2226
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax192.2 Å
Rg (real space) rg_real53.98 Å
Rg uncertainty (real space) rg_real_error2.53 Å
I(0) (real space) i0_real9.2730e+08
I(0) uncertainty (real space) i0_real_error2.0460e+07
Rg (reciprocal space) rg_reciprocal52.84 Å
I(0) (reciprocal space) i0_reciprocal925800000.0000
Solution quality estimate total_estimate0.7703
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary46.4 Å
Skewness Skewness skewness0.676
Kurtosis Kurtosis kurtosis-0.109
Angular range angular_range— – 0.1450 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha68250000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.553; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.828; Smooth: 0.524
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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9. Files and Curves (10)