9gz1

Beta-cardiac myosin interacting heads motif complexed to mavacamten

Method: ELECTRON MICROSCOPY Dmax: 170.7 Å Quality: GOOD

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

Myosin-7

Homo sapiens

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 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain A; UniProt 2–1138 Chain B; UniProt 2–1138 Not recorded Myosin light chain 1/3, skeletal muscle isoform × 2 (P05977) Myosin regulatory light chain 11 × 2 (P97457) MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 XB2 Mavacamten × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

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 1–1137; UniProt 2–1138 Author chain B; PDBConstruct 1–1137; UniProt 2–1138

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 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain C; UniProt 2–188 Chain E; UniProt 2–188 Not recorded Myosin-7 × 2 (P12883) Myosin regulatory light chain 11 × 2 (P97457) MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 XB2 Mavacamten × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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 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 1–187; UniProt 2–188 Author chain E; PDBConstruct 1–187; UniProt 2–188

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 Protein heterocomplex Heteromer Protein × 6 PDB declaration: hexameric(6) Consistent with protein copy count Chain D; UniProt 2–169 Chain F; UniProt 2–169 Not recorded Myosin-7 × 2 (P12883) Myosin light chain 1/3, skeletal muscle isoform × 2 (P05977) MG MAGNESIUM ION × 4 ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 XB2 Mavacamten × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 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.

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 D; PDBConstruct 1–168; UniProt 2–169 Author chain F; PDBConstruct 1–168; UniProt 2–169

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 9gz1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9gz1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9gz1
Deposition date deposition_date2024-10-03
Structure title titleBeta-cardiac myosin interacting heads motif complexed to mavacamten
Keywords keywordsMavacamten, Inhibitor, Interacting heads motif, myosin, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier52.53
Radius of gyration Rg (electron density) rg_electron52.54
Forward intensity I(0) i01077390000.00
Molecular weight molecular_weight274650.0 kDa
Excluded volume excluded_volume344240 ų
Envelope volume envelope_volume521520 ų
Hydration-shell volume shell_volume83494 ų
Envelope diameter envelope_diameter171.5
Shell Rg shell_rg54.85
Envelope Rg envelope_rg51.15
Shape Rg shape_rg52.53
Total Rg total_rg52.66
Total atoms total_atoms19295
Residues n_residues2383
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 dmax170.7
Rg (real space) rg_real52.52
Rg uncertainty (real space) rg_real_error1.41
I(0) (real space) i0_real1.0770e+09
I(0) uncertainty (real space) i0_real_error1.9820e+07
Rg (reciprocal space) rg_reciprocal52.53
I(0) (reciprocal space) i0_reciprocal1077000000.0000
Solution quality estimate total_estimate0.8350
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary62.6
Skewness Skewness skewness0.224
Kurtosis Kurtosis kurtosis-0.648
Angular range angular_range— – 0.1500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha79860000.0000
Real-space data points n_real_points31
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.950; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)