9yop

Cryo-EM structure of human beta-cardiac myosin in the interacting-heads motif and S2-FH docked state

Method: ELECTRON MICROSCOPY Dmax: 184.5 Å Quality: GOOD

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

Myosin-7,General control transcription factor GCN4,Enhanced Green fluorescent protein

Aequorea victoria

UniProt P03069

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 250–281 Chain B; UniProt 250–281 Not recorded Myosin light chain 1/3, skeletal muscle isoform × 2 (P05977) Myosin regulatory light chain 11 × 2 (P97457) ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

162 other PDB entries and 200 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GCN4_YEAST
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1017–1048; UniProt 250–281 Author chain B; PDBConstruct 1017–1048; UniProt 250–281

Myosin-7,General control transcription factor GCN4,Enhanced Green fluorescent protein

Aequorea victoria

UniProt P12883

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–1016 Chain B; UniProt 1–1016 Not recorded Myosin light chain 1/3, skeletal muscle isoform × 2 (P05977) Myosin regulatory light chain 11 × 2 (P97457) ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

40 other PDB entries and 55 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYH7_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1016; UniProt 1–1016 Author chain B; PDBConstruct 1–1016; UniProt 1–1016

Myosin-7,General control transcription factor GCN4,Enhanced Green fluorescent protein

Aequorea victoria

UniProt P42212

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 1–238 Chain B; UniProt 1–238 Not recorded Myosin light chain 1/3, skeletal muscle isoform × 2 (P05977) Myosin regulatory light chain 11 × 2 (P97457) ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

568 other PDB entries and 744 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GFP_AEQVI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1055–1292; UniProt 1–238 Author chain B; PDBConstruct 1055–1292; UniProt 1–238

Myosin light chain 1/3, skeletal muscle isoform

OrganismNot specified

UniProt P05977

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 1–188 Chain D; UniProt 1–188 Not recorded Myosin-7,General control transcription factor GCN4,Enhanced Green fluorescent protein × 2 (P12883,P03069,P42212) Myosin regulatory light chain 11 × 2 (P97457) ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYL1_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–188; UniProt 1–188 Author chain D; PDBConstruct 1–188; UniProt 1–188

Myosin regulatory light chain 11

OrganismNot specified

UniProt P97457

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain E; UniProt 1–169 Chain F; UniProt 1–169 Not recorded Myosin-7,General control transcription factor GCN4,Enhanced Green fluorescent protein × 2 (P12883,P03069,P42212) Myosin light chain 1/3, skeletal muscle isoform × 2 (P05977) ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.50 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.

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

View Construct and Data Evidence
UniProt name MYL11_MOUSE
Isoform
PDB entities 3
Chains and sequence ranges Author chain E; PDBConstruct 1–169; UniProt 1–169 Author chain F; PDBConstruct 1–169; UniProt 1–169

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 9yop

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9yop
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9yop
Deposition date deposition_date2025-10-13
Structure title titleCryo-EM structure of human beta-cardiac myosin in the interacting-heads motif and S2-FH docked state
Keywords keywordsCardiac Myosin, Interacting Heads Motif, Contractile Protein, Actin Binding; CONTRACTILE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.53
Radius of gyration Rg (electron density) rg_electron53.65
Forward intensity I(0) i01092210000.00
Molecular weight molecular_weight277020.0 kDa
Excluded volume excluded_volume347390 ų
Envelope volume envelope_volume519930 ų
Hydration-shell volume shell_volume82288 ų
Envelope diameter envelope_diameter181.3
Shell Rg shell_rg54.90
Envelope Rg envelope_rg52.15
Shape Rg shape_rg53.64
Total Rg total_rg53.74
Total atoms total_atoms19465
Residues n_residues2411
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 dmax184.5
Rg (real space) rg_real53.54
Rg uncertainty (real space) rg_real_error1.53
I(0) (real space) i0_real1.0920e+09
I(0) uncertainty (real space) i0_real_error1.8450e+07
Rg (reciprocal space) rg_reciprocal53.50
I(0) (reciprocal space) i0_reciprocal1092000000.0000
Solution quality estimate total_estimate0.8897
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary63.6
Skewness Skewness skewness0.253
Kurtosis Kurtosis kurtosis-0.574
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha76200000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.887; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.903

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)