4a7f

Structure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 3)

Method: ELECTRON MICROSCOPY Dmax: 215.1 Å Quality: GOOD

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain A; UniProt 3–377 Chain D; UniProt 3–377 Chain E; UniProt 3–377 Chain F; UniProt 3–377 Chain I; UniProt 3–377 Non-standard monomer:Yes (specific site not provided by mmCIF) TROPOMYOSIN 1 ALPHA × 2 (P58772) MYOSIN IE HEAVY CHAIN × 3 (Q03479) ADP ADENOSINE-5'-DIPHOSPHATE × 5 CA CALCIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:5 MM HEPES-OH, 100 MM KCL, 2 MM MGCL2, 50 MM GLUTAMINE, 50 MM ARGININE;pH 7.2;5 MM HEPES-OH, 100 MM KCL, 2 MM MGCL2, 50 MM GLUTAMINE, 50 MM ARGININE cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 7.70 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 A; PDBConstruct 1–375; UniProt 3–377 Author chain D; PDBConstruct 1–375; UniProt 3–377 Author chain E; PDBConstruct 1–375; UniProt 3–377 Author chain F; PDBConstruct 1–375; UniProt 3–377 Author chain I; PDBConstruct 1–375; UniProt 3–377

TROPOMYOSIN 1 ALPHA

ORYCTOLAGUS CUNICULUS

UniProt P58772

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain B; UniProt 98–233 Chain H; UniProt 98–233 Fragment:RESIDUES 98-233 ACTIN, ALPHA SKELETAL MUSCLE × 5 (P68135) MYOSIN IE HEAVY CHAIN × 3 (Q03479) ADP ADENOSINE-5'-DIPHOSPHATE × 5 CA CALCIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:5 MM HEPES-OH, 100 MM KCL, 2 MM MGCL2, 50 MM GLUTAMINE, 50 MM ARGININE;pH 7.2;5 MM HEPES-OH, 100 MM KCL, 2 MM MGCL2, 50 MM GLUTAMINE, 50 MM ARGININE cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 7.70 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.

10 other PDB entries and 20 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TPM1_RABIT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–136; UniProt 98–233 Author chain H; PDBConstruct 1–136; UniProt 98–233

MYOSIN IE HEAVY CHAIN

DICTYOSTELIUM DISCOIDEUM

UniProt Q03479

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 × 10 PDB declaration: decameric(10) Consistent with protein copy count Chain C; UniProt 1–697 Chain G; UniProt 1–697 Chain J; UniProt 1–697 Fragment:RESIDUES 1-697 Mutation:YES ACTIN, ALPHA SKELETAL MUSCLE × 5 (P68135) TROPOMYOSIN 1 ALPHA × 2 (P58772) ADP ADENOSINE-5'-DIPHOSPHATE × 5 CA CALCIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:5 MM HEPES-OH, 100 MM KCL, 2 MM MGCL2, 50 MM GLUTAMINE, 50 MM ARGININE;pH 7.2;5 MM HEPES-OH, 100 MM KCL, 2 MM MGCL2, 50 MM GLUTAMINE, 50 MM ARGININE cryo-EM vitrification conditions:Cryogen ETHANE;LIQUID ETHANE Resolution 7.70 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.

3 other PDB entries and 6 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYOE_DICDI
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–697; UniProt 1–697 Author chain G; PDBConstruct 1–697; UniProt 1–697 Author chain J; PDBConstruct 1–697; UniProt 1–697

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 4a7f

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4a7f
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4a7f
Deposition date deposition_date2011-11-14
Structure title titleStructure of the Actin-Tropomyosin-Myosin Complex (rigor ATM 3)
Keywords keywords;STRUCTURAL PROTEIN-HYDROLASE COMPLEX, STRUCTURAL PROTEIN, CYTOSKELETON, CONTRACTILE FILAMENT, MOTOR ACTIVITY, MYOSIN BINDING, ACTIN BINDING, ATP CATABOLIC PROCESS, RIGOR STATE ;; STRUCTURAL PROTEIN/HYDROLASE
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier61.88
Radius of gyration Rg (electron density) rg_electron61.87
Forward intensity I(0) i03284320000.00
Molecular weight molecular_weight477610.0 kDa
Excluded volume excluded_volume596050 ų
Envelope volume envelope_volume957230 ų
Hydration-shell volume shell_volume129040 ų
Envelope diameter envelope_diameter222.0
Shell Rg shell_rg62.83
Envelope Rg envelope_rg60.59
Shape Rg shape_rg61.88
Total Rg total_rg61.86
Total atoms total_atoms33500
Residues n_residues4209
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 dmax215.1
Rg (real space) rg_real61.91
Rg uncertainty (real space) rg_real_error2.75
I(0) (real space) i0_real3.2840e+09
I(0) uncertainty (real space) i0_real_error7.0920e+07
Rg (reciprocal space) rg_reciprocal61.81
I(0) (reciprocal space) i0_reciprocal3284000000.0000
Solution quality estimate total_estimate0.8697
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary68.8
Skewness Skewness skewness0.337
Kurtosis Kurtosis kurtosis-0.406
Angular range angular_range— – 0.1250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha239400000.0000
Real-space data points n_real_points26
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.824; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.837

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)