8r9v

CryoEM structure of the primed actomyosin-5a complex

Method: ELECTRON MICROSCOPY Dmax: 154.2 Å Quality: GOOD

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

Unconventional myosin-Va

Mus musculus

UniProt Q99104

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 1–797 Mutation:S217A, Deletion DDEK 594-597 Actin, alpha skeletal muscle × 3 (P68135) PO4 PHOSPHATE ION × 1 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE;F-actin was mixed with myosin-5a (S1 1 IQ motif, residues 1-797, S217A, DDEK 594-597 deletion) that had been pre-incubated with ATP, and vitrified at 10 ms post-mixing Resolution 4.40 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.

8 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYO5A_MOUSE
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–793; UniProt 1–797

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 heterocomplex Heteromer Protein × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 3–377 Chain C; UniProt 3–377 Chain D; UniProt 3–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Unconventional myosin-Va × 1 (Q99104) PO4 PHOSPHATE ION × 1 MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE;F-actin was mixed with myosin-5a (S1 1 IQ motif, residues 1-797, S217A, DDEK 594-597 deletion) that had been pre-incubated with ATP, and vitrified at 10 ms post-mixing Resolution 4.40 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–376; UniProt 3–377 Author chain C; PDBConstruct 2–376; UniProt 3–377 Author chain D; PDBConstruct 2–376; UniProt 3–377

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 8r9v

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8r9v
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8r9v
Deposition date deposition_date2023-11-30
Structure title titleCryoEM structure of the primed actomyosin-5a complex
Keywords keywordsMyosin, Actin, Actomyosin, Primed actomyosin, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier45.49
Radius of gyration Rg (electron density) rg_electron45.37
Forward intensity I(0) i0660630000.00
Molecular weight molecular_weight211610.0 kDa
Excluded volume excluded_volume264490 ų
Envelope volume envelope_volume376710 ų
Hydration-shell volume shell_volume68532 ų
Envelope diameter envelope_diameter162.2
Shell Rg shell_rg50.23
Envelope Rg envelope_rg44.85
Shape Rg shape_rg45.37
Total Rg total_rg45.59
Total atoms total_atoms14851
Residues n_residues1857
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 dmax154.2
Rg (real space) rg_real45.47
Rg uncertainty (real space) rg_real_error2.08
I(0) (real space) i0_real6.6060e+08
I(0) uncertainty (real space) i0_real_error1.5110e+07
Rg (reciprocal space) rg_reciprocal45.49
I(0) (reciprocal space) i0_reciprocal660600000.0000
Solution quality estimate total_estimate0.8904
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary52.9
Skewness Skewness skewness0.276
Kurtosis Kurtosis kurtosis-0.456
Angular range angular_range— – 0.1750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha61890000.0000
Real-space data points n_real_points36
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.885; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.981; Smooth: 0.937

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)