7sxa

T-Plastin-F-actin complex, pre-bundling intermediate state

Method: ELECTRON MICROSCOPY Dmax: 132.2 Å Quality: GOOD

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

Plastin-3

Homo sapiens

UniProt P13797

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 1–630 Not recorded Actin, alpha skeletal muscle × 3 (P68139) ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.87 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.

5 other PDB entries and 5 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name PLST_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–630; UniProt 1–630

Actin, alpha skeletal muscle

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 1–377 Chain C; UniProt 1–377 Chain D; UniProt 1–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Plastin-3 × 1 (P13797) ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.87 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 2
Chains and sequence ranges 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

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 7sxa

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7sxa
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7sxa
Deposition date deposition_date2021-11-22
Structure title titleT-Plastin-F-actin complex, pre-bundling intermediate state
Keywords keywordsT-plastin, plastin, actin, filopodium, cytoskeleton, cell protrusion, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier40.38
Radius of gyration Rg (electron density) rg_electron40.05
Forward intensity I(0) i0394453000.00
Molecular weight molecular_weight160750.0 kDa
Excluded volume excluded_volume200660 ų
Envelope volume envelope_volume267560 ų
Hydration-shell volume shell_volume55983 ų
Envelope diameter envelope_diameter140.4
Shell Rg shell_rg45.16
Envelope Rg envelope_rg39.79
Shape Rg shape_rg40.06
Total Rg total_rg40.28
Total atoms total_atoms11272
Residues n_residues1428
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 dmax132.2
Rg (real space) rg_real40.38
Rg uncertainty (real space) rg_real_error1.14
I(0) (real space) i0_real3.9450e+08
I(0) uncertainty (real space) i0_real_error7.2420e+06
Rg (reciprocal space) rg_reciprocal40.38
I(0) (reciprocal space) i0_reciprocal394500000.0000
Solution quality estimate total_estimate0.8881
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary44.1
Skewness Skewness skewness0.306
Kurtosis Kurtosis kurtosis-0.427
Angular range angular_range— – 0.1950 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37430000.0000
Real-space data points n_real_points40
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.988; Smooth: 0.790

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)