7udt

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

Method: ELECTRON MICROSCOPY Dmax: 172.4 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 × 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) regulatory light chain × 1 Unconventional myosin-XV × 1 (Q9QZZ4) ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 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 3.17 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 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 regulatory light chain × 1 Actin, alpha skeletal muscle × 3 (P68139) ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 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 3.17 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 3
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 7udt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7udt
Deposition date deposition_date2022-03-20
Structure title titlecryo-EM structure of the rigor 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_guinier49.26
Radius of gyration Rg (electron density) rg_electron49.33
Forward intensity I(0) i0729709000.00
Molecular weight molecular_weight223350.0 kDa
Excluded volume excluded_volume279330 ų
Envelope volume envelope_volume410700 ų
Hydration-shell volume shell_volume70413 ų
Envelope diameter envelope_diameter189.0
Shell Rg shell_rg51.65
Envelope Rg envelope_rg49.54
Shape Rg shape_rg49.33
Total Rg total_rg49.42
Total atoms total_atoms15683
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 dmax172.4
Rg (real space) rg_real49.57
Rg uncertainty (real space) rg_real_error1.85
I(0) (real space) i0_real7.2970e+08
I(0) uncertainty (real space) i0_real_error1.4320e+07
Rg (reciprocal space) rg_reciprocal49.26
I(0) (reciprocal space) i0_reciprocal729400000.0000
Solution quality estimate total_estimate0.6487
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary53.9
Skewness Skewness skewness0.457
Kurtosis Kurtosis kurtosis-0.204
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha62110000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.833; Stabil: 1.000; Sysdev: 0.087; Positv: 1.000; Valcen: 0.941; Smooth: 0.728

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id7udtG01
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand
Domain ID domain_id7udtG02
Class class1 — Mainly Alpha
Architecture architecture10 — Orthogonal Bundle
Topology topology238 — Recoverin; domain 1
Homologous superfamily homologous superfamily10 — EF-hand

8. Citations (1)

9. Files and Curves (10)