3j8k

Tilted state of actin, T2

Method: ELECTRON MICROSCOPY Dmax: 241.7 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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 1–377 Chain B; UniProt 1–377 Chain C; UniProt 1–377 Chain D; UniProt 1–377 Chain E; UniProt 1–377 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 Not recorded No other associated polymer ELECTRON MICROSCOPY cryo-EM vitrification conditions:Cryogen ETHANE Resolution 12.00 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 1–377; UniProt 1–377 Author chain B; PDBConstruct 1–377; UniProt 1–377 Author chain C; PDBConstruct 1–377; UniProt 1–377 Author chain D; PDBConstruct 1–377; UniProt 1–377 Author chain E; PDBConstruct 1–377; UniProt 1–377 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 3j8k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3j8k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3j8k
Deposition date deposition_date2014-11-07
Structure title titleTilted state of actin, T2
Keywords keywordshelical polymer, actin filament, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier86.23
Radius of gyration Rg (electron density) rg_electron88.78
Forward intensity I(0) i02485100000.00
Molecular weight molecular_weight418040.0 kDa
Excluded volume excluded_volume522250 ų
Envelope volume envelope_volume857680 ų
Hydration-shell volume shell_volume97200 ų
Envelope diameter envelope_diameter334.4
Shell Rg shell_rg58.24
Envelope Rg envelope_rg88.40
Shape Rg shape_rg88.78
Total Rg total_rg88.21
Total atoms total_atoms29330
Residues n_residues3750
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 dmax241.7
Rg (real space) rg_real79.86
Rg uncertainty (real space) rg_real_error1.55
I(0) (real space) i0_real2.3800e+09
I(0) uncertainty (real space) i0_real_error4.9900e+07
Rg (reciprocal space) rg_reciprocal78.99
I(0) (reciprocal space) i0_reciprocal2434000000.0000
Solution quality estimate total_estimate0.8347
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.7
Skewness Skewness skewness0.481
Kurtosis Kurtosis kurtosis-0.749
Angular range angular_range— – 0.0900 −1
Current regularization parameter α current_alpha0.6157
Highest regularization parameter α highest_alpha94610000.0000
Real-space data points n_real_points19
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.694; Stabil: 0.969; Sysdev: 1.000; Positv: 1.000; Valcen: 0.896; Smooth: 0.011

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

8. Citations (1)

9. Files and Curves (10)