8d16

Bent ADP-Pi-F-actin

Method: ELECTRON MICROSCOPY Dmax: 209.5 Å Quality: REASONABLE

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

Actin, alpha skeletal muscle, intermediate form

OrganismNot specified

UniProt P68139

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 7–377 Chain B; UniProt 7–377 Chain C; UniProt 7–377 Chain D; UniProt 7–377 Chain E; UniProt 7–377 Chain F; UniProt 7–377 Chain G; UniProt 7–377 Non-standard monomer:Yes (specific site not provided by mmCIF) ADP ADENOSINE-5'-DIPHOSPHATE × 7 MG MAGNESIUM ION × 7 PO4 PHOSPHATE ION × 7 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.71 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.

57 other PDB entries and 66 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_CHICK
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 C; PDBConstruct 1–371; UniProt 7–377 Author chain D; 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 G; 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 8d16

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8d16
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8d16
Deposition date deposition_date2022-05-26
Structure title titleBent ADP-Pi-F-actin
Keywords keywordsCytoskeleton, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.28
Radius of gyration Rg (electron density) rg_electron61.75
Forward intensity I(0) i01267620000.00
Molecular weight molecular_weight293170.0 kDa
Excluded volume excluded_volume365110 ų
Envelope volume envelope_volume510070 ų
Hydration-shell volume shell_volume77061 ų
Envelope diameter envelope_diameter241.1
Shell Rg shell_rg52.07
Envelope Rg envelope_rg62.01
Shape Rg shape_rg61.76
Total Rg total_rg61.45
Total atoms total_atoms20531
Residues n_residues2590
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 dmax209.5
Rg (real space) rg_real61.39
Rg uncertainty (real space) rg_real_error2.00
I(0) (real space) i0_real1.2670e+09
I(0) uncertainty (real space) i0_real_error2.5810e+07
Rg (reciprocal space) rg_reciprocal59.28
I(0) (reciprocal space) i0_reciprocal1263000000.0000
Solution quality estimate total_estimate0.7443
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary48.4
Skewness Skewness skewness0.687
Kurtosis Kurtosis kurtosis-0.213
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0003
Highest regularization parameter α highest_alpha77680000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.535; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.866; Smooth: 0.202

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)