8g4l

Cryo-EM structure of the human cardiac myosin filament

Method: ELECTRON MICROSCOPY Dmax: 481.2 Å Quality: GOOD

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

Myosin-7

OrganismNot specified

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 × 123 PDB declaration: 123-meric(123) Consistent with protein copy count Chain A; UniProt 1–1935 Chain AA; UniProt 1–1935 Chain AB; UniProt 1–1935 Chain AG; UniProt 1–1935 Chain AH; UniProt 1–1935 Chain AI; UniProt 1–1935 Chain AJ; UniProt 1–1935 Chain AK; UniProt 1–1935 Chain AL; UniProt 1–1935 Chain AM; UniProt 1–1935 Chain AN; UniProt 1–1935 Chain AO; UniProt 1–1935 Chain AP; UniProt 1–1935 Chain AQ; UniProt 1–1935 Chain AR; UniProt 1–1935 Chain AS; UniProt 1–1935 Chain AT; UniProt 1–1935 Chain AU; UniProt 1–1935 Chain AV; UniProt 1–1935 Chain AW; UniProt 1–1935 Chain AX; UniProt 1–1935 Chain AY; UniProt 1–1935 Chain AZ; UniProt 1–1935 Chain B; UniProt 1–1935 Chain BA; UniProt 1–1935 Chain BB; UniProt 1–1935 Chain BG; UniProt 1–1935 Chain BH; UniProt 1–1935 Chain BI; UniProt 1–1935 Chain BJ; UniProt 1–1935 Chain BK; UniProt 1–1935 Chain BL; UniProt 1–1935 Chain BM; UniProt 1–1935 Chain BN; UniProt 1–1935 Chain BO; UniProt 1–1935 Chain BP; UniProt 1–1935 Chain BQ; UniProt 1–1935 Chain BR; UniProt 1–1935 Chain BS; UniProt 1–1935 Chain BT; UniProt 1–1935 Chain BU; UniProt 1–1935 Chain BV; UniProt 1–1935 Chain BW; UniProt 1–1935 Chain BX; UniProt 1–1935 Chain BY; UniProt 1–1935 Chain BZ; UniProt 1–1935 Chain G; UniProt 1–1935 Chain H; UniProt 1–1935 Chain I; UniProt 1–1935 Chain J; UniProt 1–1935 Chain K; UniProt 1–1935 Chain L; UniProt 1–1935 Chain M; UniProt 1–1935 Chain N; UniProt 1–1935 Chain O; UniProt 1–1935 Chain P; UniProt 1–1935 Chain Q; UniProt 1–1935 Chain R; UniProt 1–1935 Chain S; UniProt 1–1935 Chain T; UniProt 1–1935 Chain U; UniProt 1–1935 Chain V; UniProt 1–1935 Chain W; UniProt 1–1935 Chain X; UniProt 1–1935 Chain Y; UniProt 1–1935 Chain Z; UniProt 1–1935 Chain ae; UniProt 1–1935 Chain af; UniProt 1–1935 Chain ak; UniProt 1–1935 Chain al; UniProt 1–1935 Chain be; UniProt 1–1935 Chain bf; UniProt 1–1935 Chain bk; UniProt 1–1935 Chain bl; UniProt 1–1935 Chain e; UniProt 1–1935 Chain f; UniProt 1–1935 Chain k; UniProt 1–1935 Chain l; UniProt 1–1935 Not recorded Myosin light chain 3 × 18 (P08590) Myosin regulatory light chain 2, ventricular/cardiac muscle isoform × 18 (P10916) Titin × 6 (Q8WZ42) Myosin-binding protein C, cardiac-type × 3 (Q14896) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.40 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 1–1935; UniProt 1–1935 Author chain AA; PDBConstruct 1–1935; UniProt 1–1935 Author chain AB; PDBConstruct 1–1935; UniProt 1–1935 Author chain AG; PDBConstruct 1–1935; UniProt 1–1935 Author chain AH; PDBConstruct 1–1935; UniProt 1–1935 Author chain AI; PDBConstruct 1–1935; UniProt 1–1935 Author chain AJ; PDBConstruct 1–1935; UniProt 1–1935 Author chain AK; PDBConstruct 1–1935; UniProt 1–1935 Author chain AL; PDBConstruct 1–1935; UniProt 1–1935 Author chain AM; PDBConstruct 1–1935; UniProt 1–1935 Author chain AN; PDBConstruct 1–1935; UniProt 1–1935 Author chain AO; PDBConstruct 1–1935; UniProt 1–1935 Author chain AP; PDBConstruct 1–1935; UniProt 1–1935 Author chain AQ; PDBConstruct 1–1935; UniProt 1–1935 Author chain AR; PDBConstruct 1–1935; UniProt 1–1935 Author chain AS; PDBConstruct 1–1935; UniProt 1–1935 Author chain AT; PDBConstruct 1–1935; UniProt 1–1935 Author chain AU; PDBConstruct 1–1935; UniProt 1–1935 Author chain AV; PDBConstruct 1–1935; UniProt 1–1935 Author chain AW; PDBConstruct 1–1935; UniProt 1–1935 Author chain AX; PDBConstruct 1–1935; UniProt 1–1935 Author chain AY; PDBConstruct 1–1935; UniProt 1–1935 Author chain AZ; PDBConstruct 1–1935; UniProt 1–1935 Author chain B; PDBConstruct 1–1935; UniProt 1–1935 Author chain BA; PDBConstruct 1–1935; UniProt 1–1935 Author chain BB; PDBConstruct 1–1935; UniProt 1–1935 Author chain BG; PDBConstruct 1–1935; UniProt 1–1935 Author chain BH; PDBConstruct 1–1935; UniProt 1–1935 Author chain BI; PDBConstruct 1–1935; UniProt 1–1935 Author chain BJ; PDBConstruct 1–1935; UniProt 1–1935 Author chain BK; PDBConstruct 1–1935; UniProt 1–1935 Author chain BL; PDBConstruct 1–1935; UniProt 1–1935 Author chain BM; PDBConstruct 1–1935; UniProt 1–1935 Author chain BN; PDBConstruct 1–1935; UniProt 1–1935 Author chain BO; PDBConstruct 1–1935; UniProt 1–1935 Author chain BP; PDBConstruct 1–1935; UniProt 1–1935 Author chain BQ; PDBConstruct 1–1935; UniProt 1–1935 Author chain BR; PDBConstruct 1–1935; UniProt 1–1935 Author chain BS; PDBConstruct 1–1935; UniProt 1–1935 Author chain BT; PDBConstruct 1–1935; UniProt 1–1935 Author chain BU; PDBConstruct 1–1935; UniProt 1–1935 Author chain BV; PDBConstruct 1–1935; UniProt 1–1935 Author chain BW; PDBConstruct 1–1935; UniProt 1–1935 Author chain BX; PDBConstruct 1–1935; UniProt 1–1935 Author chain BY; PDBConstruct 1–1935; UniProt 1–1935 Author chain BZ; PDBConstruct 1–1935; UniProt 1–1935 Author chain G; PDBConstruct 1–1935; UniProt 1–1935 Author chain H; PDBConstruct 1–1935; UniProt 1–1935 Author chain I; PDBConstruct 1–1935; UniProt 1–1935 Author chain J; PDBConstruct 1–1935; UniProt 1–1935 Author chain K; PDBConstruct 1–1935; UniProt 1–1935 Author chain L; PDBConstruct 1–1935; UniProt 1–1935 Author chain M; PDBConstruct 1–1935; UniProt 1–1935 Author chain N; PDBConstruct 1–1935; UniProt 1–1935 Author chain O; PDBConstruct 1–1935; UniProt 1–1935 Author chain P; PDBConstruct 1–1935; UniProt 1–1935 Author chain Q; PDBConstruct 1–1935; UniProt 1–1935 Author chain R; PDBConstruct 1–1935; UniProt 1–1935 Author chain S; PDBConstruct 1–1935; UniProt 1–1935 Author chain T; PDBConstruct 1–1935; UniProt 1–1935 Author chain U; PDBConstruct 1–1935; UniProt 1–1935 Author chain V; PDBConstruct 1–1935; UniProt 1–1935 Author chain W; PDBConstruct 1–1935; UniProt 1–1935 Author chain X; PDBConstruct 1–1935; UniProt 1–1935 Author chain Y; PDBConstruct 1–1935; UniProt 1–1935 Author chain Z; PDBConstruct 1–1935; UniProt 1–1935 Author chain ae; PDBConstruct 1–1935; UniProt 1–1935 Author chain af; PDBConstruct 1–1935; UniProt 1–1935 Author chain ak; PDBConstruct 1–1935; UniProt 1–1935 Author chain al; PDBConstruct 1–1935; UniProt 1–1935 Author chain be; PDBConstruct 1–1935; UniProt 1–1935 Author chain bf; PDBConstruct 1–1935; UniProt 1–1935 Author chain bk; PDBConstruct 1–1935; UniProt 1–1935 Author chain bl; PDBConstruct 1–1935; UniProt 1–1935 Author chain e; PDBConstruct 1–1935; UniProt 1–1935 Author chain f; PDBConstruct 1–1935; UniProt 1–1935 Author chain k; PDBConstruct 1–1935; UniProt 1–1935 Author chain l; PDBConstruct 1–1935; UniProt 1–1935

Myosin light chain 3

OrganismNot specified

UniProt P08590

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 × 123 PDB declaration: 123-meric(123) Consistent with protein copy count Chain AE; UniProt 1–195 Chain AF; UniProt 1–195 Chain BE; UniProt 1–195 Chain BF; UniProt 1–195 Chain E; UniProt 1–195 Chain F; UniProt 1–195 Chain a; UniProt 1–195 Chain aa; UniProt 1–195 Chain ab; UniProt 1–195 Chain ag; UniProt 1–195 Chain ah; UniProt 1–195 Chain b; UniProt 1–195 Chain ba; UniProt 1–195 Chain bb; UniProt 1–195 Chain bg; UniProt 1–195 Chain bh; UniProt 1–195 Chain g; UniProt 1–195 Chain h; UniProt 1–195 Not recorded Myosin-7 × 78 (P12883) Myosin regulatory light chain 2, ventricular/cardiac muscle isoform × 18 (P10916) Titin × 6 (Q8WZ42) Myosin-binding protein C, cardiac-type × 3 (Q14896) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.40 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYL3_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain AE; PDBConstruct 1–195; UniProt 1–195 Author chain AF; PDBConstruct 1–195; UniProt 1–195 Author chain BE; PDBConstruct 1–195; UniProt 1–195 Author chain BF; PDBConstruct 1–195; UniProt 1–195 Author chain E; PDBConstruct 1–195; UniProt 1–195 Author chain F; PDBConstruct 1–195; UniProt 1–195 Author chain a; PDBConstruct 1–195; UniProt 1–195 Author chain aa; PDBConstruct 1–195; UniProt 1–195 Author chain ab; PDBConstruct 1–195; UniProt 1–195 Author chain ag; PDBConstruct 1–195; UniProt 1–195 Author chain ah; PDBConstruct 1–195; UniProt 1–195 Author chain b; PDBConstruct 1–195; UniProt 1–195 Author chain ba; PDBConstruct 1–195; UniProt 1–195 Author chain bb; PDBConstruct 1–195; UniProt 1–195 Author chain bg; PDBConstruct 1–195; UniProt 1–195 Author chain bh; PDBConstruct 1–195; UniProt 1–195 Author chain g; PDBConstruct 1–195; UniProt 1–195 Author chain h; PDBConstruct 1–195; UniProt 1–195

Myosin regulatory light chain 2, ventricular/cardiac muscle isoform

OrganismNot specified

UniProt P10916

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 × 123 PDB declaration: 123-meric(123) Consistent with protein copy count Chain ac; UniProt 1–166 Chain ad; UniProt 1–166 Chain ai; UniProt 1–166 Chain aj; UniProt 1–166 Chain aq; UniProt 1–166 Chain ar; UniProt 1–166 Chain bc; UniProt 1–166 Chain bd; UniProt 1–166 Chain bi; UniProt 1–166 Chain bj; UniProt 1–166 Chain bq; UniProt 1–166 Chain br; UniProt 1–166 Chain c; UniProt 1–166 Chain d; UniProt 1–166 Chain i; UniProt 1–166 Chain j; UniProt 1–166 Chain q; UniProt 1–166 Chain r; UniProt 1–166 Not recorded Myosin-7 × 78 (P12883) Myosin light chain 3 × 18 (P08590) Titin × 6 (Q8WZ42) Myosin-binding protein C, cardiac-type × 3 (Q14896) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.40 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MLRV_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain ac; PDBConstruct 1–166; UniProt 1–166 Author chain ad; PDBConstruct 1–166; UniProt 1–166 Author chain ai; PDBConstruct 1–166; UniProt 1–166 Author chain aj; PDBConstruct 1–166; UniProt 1–166 Author chain aq; PDBConstruct 1–166; UniProt 1–166 Author chain ar; PDBConstruct 1–166; UniProt 1–166 Author chain bc; PDBConstruct 1–166; UniProt 1–166 Author chain bd; PDBConstruct 1–166; UniProt 1–166 Author chain bi; PDBConstruct 1–166; UniProt 1–166 Author chain bj; PDBConstruct 1–166; UniProt 1–166 Author chain bq; PDBConstruct 1–166; UniProt 1–166 Author chain br; PDBConstruct 1–166; UniProt 1–166 Author chain c; PDBConstruct 1–166; UniProt 1–166 Author chain d; PDBConstruct 1–166; UniProt 1–166 Author chain i; PDBConstruct 1–166; UniProt 1–166 Author chain j; PDBConstruct 1–166; UniProt 1–166 Author chain q; PDBConstruct 1–166; UniProt 1–166 Author chain r; PDBConstruct 1–166; UniProt 1–166

Titin

OrganismNot specified

UniProt Q8WZ42

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 × 123 PDB declaration: 123-meric(123) Consistent with protein copy count Chain am; UniProt 22784–23867 Chain an; UniProt 22784–23867 Chain bm; UniProt 22784–23867 Chain bn; UniProt 22784–23867 Chain m; UniProt 22784–23867 Chain n; UniProt 22784–23867 Not recorded Myosin-7 × 78 (P12883) Myosin light chain 3 × 18 (P08590) Myosin regulatory light chain 2, ventricular/cardiac muscle isoform × 18 (P10916) Myosin-binding protein C, cardiac-type × 3 (Q14896) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.40 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.

54 other PDB entries and 123 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TITIN_HUMAN
Isoform
PDB entities 4
Chains and sequence ranges Author chain am; PDBConstruct 1–1084; UniProt 22784–23867 Author chain an; PDBConstruct 1–1084; UniProt 22784–23867 Author chain bm; PDBConstruct 1–1084; UniProt 22784–23867 Author chain bn; PDBConstruct 1–1084; UniProt 22784–23867 Author chain m; PDBConstruct 1–1084; UniProt 22784–23867 Author chain n; PDBConstruct 1–1084; UniProt 22784–23867

Myosin-binding protein C, cardiac-type

OrganismNot specified

UniProt Q14896

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 × 123 PDB declaration: 123-meric(123) Consistent with protein copy count Chain ao; UniProt 1–1274 Chain bo; UniProt 1–1274 Chain o; UniProt 1–1274 Not recorded Myosin-7 × 78 (P12883) Myosin light chain 3 × 18 (P08590) Myosin regulatory light chain 2, ventricular/cardiac muscle isoform × 18 (P10916) Titin × 6 (Q8WZ42) ELECTRON MICROSCOPY cryo-EM buffer:pH 6.8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 6.40 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.

16 other PDB entries and 16 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYPC3_HUMAN
Isoform
PDB entities 5
Chains and sequence ranges Author chain ao; PDBConstruct 1–1274; UniProt 1–1274 Author chain bo; PDBConstruct 1–1274; UniProt 1–1274 Author chain o; PDBConstruct 1–1274; UniProt 1–1274

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 8g4l

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8g4l
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8g4l
Deposition date deposition_date2023-02-10
Structure title titleCryo-EM structure of the human cardiac myosin filament
Keywords keywordscardiac, myosin, filament, complex, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier
Radius of gyration Rg (electron density) rg_electron167.90
Forward intensity I(0) i0489957000000.00
Molecular weight molecular_weight5895500.0 kDa
Excluded volume excluded_volume7344000 ų
Envelope volume envelope_volume16577000 ų
Hydration-shell volume shell_volume840770 ų
Envelope diameter envelope_diameter579.0
Shell Rg shell_rg150.60
Envelope Rg envelope_rg159.40
Shape Rg shape_rg167.90
Total Rg total_rg167.90
Total atoms total_atoms828952
Residues n_residues51438
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 dmax481.2
Rg (real space) rg_real161.40
Rg uncertainty (real space) rg_real_error1.52
I(0) (real space) i0_real4.6510e+11
I(0) uncertainty (real space) i0_real_error1.1650e+10
Rg (reciprocal space) rg_reciprocal153.40
I(0) (reciprocal space) i0_reciprocal458100000000.0000
Solution quality estimate total_estimate0.8987
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary213.9
Skewness Skewness skewness0.385
Kurtosis Kurtosis kurtosis-0.381
Angular range angular_range— – 0.0450 −1
Current regularization parameter α current_alpha1.5260
Highest regularization parameter α highest_alpha51220000000.0000
Real-space data points n_real_points10
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.078; Oscil: 0.974; Stabil: 0.942; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)