7rb8

cryo-EM structure of the ADP state wild type myosin-15-F-actin complex

Method: ELECTRON MICROSCOPY Dmax: 147.4 Å Quality: REASONABLE

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

Actin, alpha skeletal muscle, intermediate form

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 A; UniProt 5–377 Chain B; UniProt 5–377 Chain C; UniProt 5–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Isoform 3 of Unconventional myosin-XV × 1 (Q9QZZ4) 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 3.63 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

Isoform 3 of 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 × 4 PDB declaration: tetrameric(4) Consistent with protein copy count Chain D; UniProt 18–702 Not recorded Actin, alpha skeletal muscle, intermediate form × 3 (P68139) 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 3.63 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 Q9QZZ4-3
PDB entities 2
Chains and sequence ranges Author chain D; PDBConstruct 1–685; UniProt 18–702

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 7rb8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7rb8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7rb8
Deposition date deposition_date2021-07-05
Structure title titlecryo-EM structure of the ADP state wild type myosin-15-F-actin complex
Keywords keywordsmyosin motor proteins, actin cytoskeleton, stereocilia, deafness, MOTOR PROTEIN, MOTOR PROTEIN-ATP Binding Protein complex; MOTOR PROTEIN/ATP Binding Protein
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.00
Radius of gyration Rg (electron density) rg_electron43.66
Forward intensity I(0) i0609133000.00
Molecular weight molecular_weight202720.0 kDa
Excluded volume excluded_volume253440 ų
Envelope volume envelope_volume353090 ų
Hydration-shell volume shell_volume66491 ų
Envelope diameter envelope_diameter149.0
Shell Rg shell_rg49.03
Envelope Rg envelope_rg43.32
Shape Rg shape_rg43.64
Total Rg total_rg43.99
Total atoms total_atoms14226
Residues n_residues1783
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 dmax147.4
Rg (real space) rg_real45.53
Rg uncertainty (real space) rg_real_error0.56
I(0) (real space) i0_real6.0710e+08
I(0) uncertainty (real space) i0_real_error1.0350e+07
Rg (reciprocal space) rg_reciprocal44.00
I(0) (reciprocal space) i0_reciprocal609200000.0000
Solution quality estimate total_estimate0.6996
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary53.2
Skewness Skewness skewness0.384
Kurtosis Kurtosis kurtosis-0.298
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha1.7080
Highest regularization parameter α highest_alpha76530000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.929; Stabil: 0.888; Sysdev: 0.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.688

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7rb8D01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily530

8. Citations (2)

9. Files and Curves (10)