7kch

Myosin XI-F-actin complex

Method: ELECTRON MICROSCOPY Dmax: 146.0 Å Quality: GOOD

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

Actin, alpha skeletal muscle

Gallus gallus

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 B; UniProt 1–377 Chain C; UniProt 1–377 Chain G; UniProt 1–377 Not recorded Unconventional myosin heavy chain × 1 (Q9SSU1) 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,1mM MgCl2, 1mM EGTA, 0.5 mM DTT, 0.01% NaN3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.33 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 B; PDBConstruct 1–377; UniProt 1–377 Author chain C; PDBConstruct 1–377; UniProt 1–377 Author chain G; PDBConstruct 1–377; UniProt 1–377

Unconventional myosin heavy chain

Chara corallina

UniProt Q9SSU1

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 14–740 Not recorded 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,1mM MgCl2, 1mM EGTA, 0.5 mM DTT, 0.01% NaN3 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 4.33 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q9SSU1_CHACB
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–735; UniProt 14–740

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 7kch

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7kch
Deposition date deposition_date2020-10-05
Structure title titleMyosin XI-F-actin complex
Keywords keywordsmyosin, actin, cytoskeleton, motor protein, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier43.58
Radius of gyration Rg (electron density) rg_electron42.79
Forward intensity I(0) i0514798000.00
Molecular weight molecular_weight173870.0 kDa
Excluded volume excluded_volume212100 ų
Envelope volume envelope_volume332440 ų
Hydration-shell volume shell_volume63891 ų
Envelope diameter envelope_diameter147.6
Shell Rg shell_rg48.18
Envelope Rg envelope_rg42.92
Shape Rg shape_rg42.89
Total Rg total_rg42.77
Total atoms total_atoms12248
Residues n_residues1805
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 dmax146.0
Rg (real space) rg_real43.55
Rg uncertainty (real space) rg_real_error1.41
I(0) (real space) i0_real5.1480e+08
I(0) uncertainty (real space) i0_real_error8.8340e+06
Rg (reciprocal space) rg_reciprocal43.58
I(0) (reciprocal space) i0_reciprocal514800000.0000
Solution quality estimate total_estimate0.8885
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary52.7
Skewness Skewness skewness0.277
Kurtosis Kurtosis kurtosis-0.456
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha60010000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.896; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.862

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)