9cfv

Cryo-EM structure of delta-NTR myosin-1c bound to F-actin

Method: ELECTRON MICROSCOPY Dmax: 181.8 Å Quality: REASONABLE

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

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 3–377 Chain C; UniProt 3–377 Chain D; UniProt 3–377 Not recorded Unconventional myosin-Ic × 1 (Q9WTI7) Calmodulin-1 × 1 (P0DP26) ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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 1
Chains and sequence ranges Author chain B; PDBConstruct 1–375; UniProt 3–377 Author chain C; PDBConstruct 1–375; UniProt 3–377 Author chain D; PDBConstruct 1–375; UniProt 3–377

Unconventional myosin-Ic

Mus musculus

UniProt Q9WTI7

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 P; UniProt 36–755 Not recorded Actin, alpha skeletal muscle × 3 (P68135) Calmodulin-1 × 1 (P0DP26) ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

4 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYO1C_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain P; PDBConstruct 1–720; UniProt 36–755

Calmodulin-1

Mus musculus

UniProt P0DP26

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 R; UniProt 1–148 Not recorded Actin, alpha skeletal muscle × 3 (P68135) Unconventional myosin-Ic × 1 (Q9WTI7) ADP ADENOSINE-5'-DIPHOSPHATE × 3 MG MAGNESIUM ION × 3 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 2.70 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CALM1_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain R; PDBConstruct 1–148; UniProt 1–148

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 9cfv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9cfv
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9cfv
Deposition date deposition_date2024-06-27
Structure title titleCryo-EM structure of delta-NTR myosin-1c bound to F-actin
Keywords keywordsF-actin, myosin, myosin-1c, cellular motility, cryo-EM, actomyosin., STRUCTURAL PROTEIN, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier49.29
Radius of gyration Rg (electron density) rg_electron49.73
Forward intensity I(0) i0737033000.00
Molecular weight molecular_weight223030.0 kDa
Excluded volume excluded_volume278310 ų
Envelope volume envelope_volume382850 ų
Hydration-shell volume shell_volume67065 ų
Envelope diameter envelope_diameter195.5
Shell Rg shell_rg50.05
Envelope Rg envelope_rg50.59
Shape Rg shape_rg49.73
Total Rg total_rg49.75
Total atoms total_atoms15664
Residues n_residues1961
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 dmax181.8
Rg (real space) rg_real50.01
Rg uncertainty (real space) rg_real_error2.61
I(0) (real space) i0_real7.3700e+08
I(0) uncertainty (real space) i0_real_error1.6560e+07
Rg (reciprocal space) rg_reciprocal49.30
I(0) (reciprocal space) i0_reciprocal736400000.0000
Solution quality estimate total_estimate0.5785
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary51.1
Skewness Skewness skewness0.661
Kurtosis Kurtosis kurtosis0.113
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha64730000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.658; Stabil: 1.000; Sysdev: 0.013; Positv: 1.000; Valcen: 0.799; Smooth: 0.704

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)