8c4e

F-actin decorated by SipA426-685

Method: ELECTRON MICROSCOPY Dmax: 221.8 Å Quality: REASONABLE

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

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 × 12 PDB declaration: 12-meric(12) 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 Non-standard monomer:Yes (specific site not provided by mmCIF) Cell invasion protein SipA × 4 (Q8VQB5) ADP ADENOSINE-5'-DIPHOSPHATE × 8 PO4 PHOSPHATE ION × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;5 mM Tris buffer, pH 7.5, 0.1 mM DTT, 0.2 mM ATP, 0.2 mM EGTA and 0.05 mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.60 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 1–377; 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

Cell invasion protein SipA

Salmonella

UniProt Q8VQB5

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 × 12 PDB declaration: 12-meric(12) Consistent with protein copy count Chain K; UniProt 425–685 Chain L; UniProt 425–685 Chain M; UniProt 425–685 Chain N; UniProt 425–685 Not recorded Actin, alpha skeletal muscle × 8 (P68139) ADP ADENOSINE-5'-DIPHOSPHATE × 8 PO4 PHOSPHATE ION × 8 MG MAGNESIUM ION × 8 ELECTRON MICROSCOPY cryo-EM buffer:pH 8;5 mM Tris buffer, pH 7.5, 0.1 mM DTT, 0.2 mM ATP, 0.2 mM EGTA and 0.05 mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.60 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SIPA_SALEN
Isoform
PDB entities 2
Chains and sequence ranges Author chain K; PDBConstruct 1–261; UniProt 425–685 Author chain L; PDBConstruct 1–261; UniProt 425–685 Author chain M; PDBConstruct 1–261; UniProt 425–685 Author chain N; PDBConstruct 1–261; UniProt 425–685

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 8c4e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8c4e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8c4e
Deposition date deposition_date2023-01-03
最后修订 last_revision2024-01-17
Structure title titleF-actin decorated by SipA426-685
Keywords keywordsSalmonella invasion, CELL INVASION; CELL INVASION
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier66.20
Radius of gyration Rg (electron density) rg_electron68.12
Forward intensity I(0) i02433270000.00
Molecular weight molecular_weight410760.0 kDa
Excluded volume excluded_volume512360 ų
Envelope volume envelope_volume679910 ų
Hydration-shell volume shell_volume92124 ų
Envelope diameter envelope_diameter265.8
Shell Rg shell_rg55.90
Envelope Rg envelope_rg68.76
Shape Rg shape_rg68.12
Total Rg total_rg67.85
Total atoms total_atoms57268
Residues n_residues3640
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 dmax221.8
Rg (real space) rg_real67.37
Rg uncertainty (real space) rg_real_error1.88
I(0) (real space) i0_real2.4280e+09
I(0) uncertainty (real space) i0_real_error5.7880e+07
Rg (reciprocal space) rg_reciprocal64.76
I(0) (reciprocal space) i0_reciprocal2420000000.0000
Solution quality estimate total_estimate0.7334
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary46.2
Skewness Skewness skewness0.645
Kurtosis Kurtosis kurtosis-0.367
Angular range angular_range— – 0.1200 −1
Current regularization parameter α current_alpha0.0217
Highest regularization parameter α highest_alpha237200000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.548; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.712; Smooth: 0.172

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)