7udu

cryo-EM structure of the ADP state wild type myosin-15-F-actin complex (symmetry expansion and re-centering)

Method: ELECTRON MICROSCOPY Dmax: 176.2 Å Quality: GOOD

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 5–377 Chain B; UniProt 5–377 Chain C; UniProt 5–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Unconventional myosin-XV × 1 (Q9QZZ4) regulatory light chain × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;10 mM imidazole pH 7.0, 50 mM KCl, 1 mM MgCl2, 1 mM EGTA, 0.5 mM DTT, 0.01% NaN3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.15 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 1–373; UniProt 5–377 Author chain B; PDBConstruct 1–373; UniProt 5–377 Author chain C; PDBConstruct 1–373; UniProt 5–377

Unconventional myosin-XV

Mus musculus

UniProt Q9QZZ4

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 1205–1923 Fragment:motor domain Actin, alpha skeletal muscle × 3 (P68139) regulatory light chain × 1 ADP ADENOSINE-5'-DIPHOSPHATE × 4 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7;10 mM imidazole pH 7.0, 50 mM KCl, 1 mM MgCl2, 1 mM EGTA, 0.5 mM DTT, 0.01% NaN3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.15 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 MYO15_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–719; UniProt 1205–1923

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 7udu

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7udu
Deposition date deposition_date2022-03-20
Structure title titlecryo-EM structure of the ADP state wild type myosin-15-F-actin complex (symmetry expansion and re-centering)
Keywords keywordsmyosin motor proteins, actin cytoskeleton, stereocilia, deafness, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.52
Radius of gyration Rg (electron density) rg_electron49.64
Forward intensity I(0) i0735572000.00
Molecular weight molecular_weight223800.0 kDa
Excluded volume excluded_volume279710 ų
Envelope volume envelope_volume422140 ų
Hydration-shell volume shell_volume71583 ų
Envelope diameter envelope_diameter187.7
Shell Rg shell_rg52.02
Envelope Rg envelope_rg50.38
Shape Rg shape_rg49.64
Total Rg total_rg49.71
Total atoms total_atoms15711
Residues n_residues1963
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 dmax176.2
Rg (real space) rg_real49.86
Rg uncertainty (real space) rg_real_error2.35
I(0) (real space) i0_real7.3560e+08
I(0) uncertainty (real space) i0_real_error1.5400e+07
Rg (reciprocal space) rg_reciprocal49.52
I(0) (reciprocal space) i0_reciprocal735200000.0000
Solution quality estimate total_estimate0.8544
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.1
Skewness Skewness skewness0.471
Kurtosis Kurtosis kurtosis-0.188
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha70440000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.801; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.921; Smooth: 0.779

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)