8uz6

The structure of the native cardiac thin filament troponin core in Ca2+-free tilted state from the lower strand

Method: ELECTRON MICROSCOPY Dmax: 128.9 Å Quality: GOOD

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

Actin, alpha cardiac muscle 1

OrganismNot specified

UniProt B6VNT8

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain A; UniProt 1–377 Chain B; UniProt 1–377 Not recorded Troponin C, slow skeletal and cardiac muscles × 1 (P63317) Troponin I, cardiac muscle × 1 (A0A4X1V710) Troponin T2, cardiac type × 1 (A0A5G2Q8N0) Tropomyosin alpha-1 chain × 2 (P42639) ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.10 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.

19 other PDB entries and 19 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name B6VNT8_PIG
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–377; UniProt 1–377 Author chain B; PDBConstruct 1–377; UniProt 1–377

Troponin C, slow skeletal and cardiac muscles

OrganismNot specified

UniProt P63317

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain C; UniProt 1–161 Not recorded Actin, alpha cardiac muscle 1 × 2 (B6VNT8) Troponin I, cardiac muscle × 1 (A0A4X1V710) Troponin T2, cardiac type × 1 (A0A5G2Q8N0) Tropomyosin alpha-1 chain × 2 (P42639) ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.10 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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TNNC1_PIG
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–161; UniProt 1–161

Troponin I, cardiac muscle

OrganismNot specified

UniProt A0A4X1V710

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain D; UniProt 1–211 Not recorded Actin, alpha cardiac muscle 1 × 2 (B6VNT8) Troponin C, slow skeletal and cardiac muscles × 1 (P63317) Troponin T2, cardiac type × 1 (A0A5G2Q8N0) Tropomyosin alpha-1 chain × 2 (P42639) ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.10 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 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A4X1V710_PIG
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–211; UniProt 1–211

Troponin T2, cardiac type

OrganismNot specified

UniProt A0A5G2Q8N0

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain E; UniProt 1–285 Not recorded Actin, alpha cardiac muscle 1 × 2 (B6VNT8) Troponin C, slow skeletal and cardiac muscles × 1 (P63317) Troponin I, cardiac muscle × 1 (A0A4X1V710) Tropomyosin alpha-1 chain × 2 (P42639) ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.10 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.

11 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name A0A5G2Q8N0_PIG
Isoform
PDB entities 4
Chains and sequence ranges Author chain E; PDBConstruct 1–285; UniProt 1–285

Tropomyosin alpha-1 chain

OrganismNot specified

UniProt P42639

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 × 7 PDB declaration: heptameric(7) Consistent with protein copy count Chain F; UniProt 1–284 Chain G; UniProt 1–284 Not recorded Actin, alpha cardiac muscle 1 × 2 (B6VNT8) Troponin C, slow skeletal and cardiac muscles × 1 (P63317) Troponin I, cardiac muscle × 1 (A0A4X1V710) Troponin T2, cardiac type × 1 (A0A5G2Q8N0) ADP ADENOSINE-5'-DIPHOSPHATE × 2 MG MAGNESIUM ION × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.10 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.

13 other PDB entries and 14 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TPM1_PIG
Isoform
PDB entities 5
Chains and sequence ranges Author chain F; PDBConstruct 1–284; UniProt 1–284 Author chain G; PDBConstruct 1–284; UniProt 1–284

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 8uz6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8uz6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8uz6
Deposition date deposition_date2023-11-14
Structure title titleThe structure of the native cardiac thin filament troponin core in Ca2+-free tilted state from the lower strand
Keywords keywordsthin filament, troponin, tropomyosin, cryo-EM, muscle structure, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier39.37
Radius of gyration Rg (electron density) rg_electron39.05
Forward intensity I(0) i0338941000.00
Molecular weight molecular_weight146020.0 kDa
Excluded volume excluded_volume181500 ų
Envelope volume envelope_volume260070 ų
Hydration-shell volume shell_volume56290 ų
Envelope diameter envelope_diameter139.5
Shell Rg shell_rg44.13
Envelope Rg envelope_rg38.70
Shape Rg shape_rg39.03
Total Rg total_rg39.40
Total atoms total_atoms10232
Residues n_residues1281
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 dmax128.9
Rg (real space) rg_real39.31
Rg uncertainty (real space) rg_real_error1.04
I(0) (real space) i0_real3.3890e+08
I(0) uncertainty (real space) i0_real_error6.2740e+06
Rg (reciprocal space) rg_reciprocal39.35
I(0) (reciprocal space) i0_reciprocal339000000.0000
Solution quality estimate total_estimate0.8931
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary45.1
Skewness Skewness skewness0.285
Kurtosis Kurtosis kurtosis-0.409
Angular range angular_range— – 0.2000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha40920000.0000
Real-space data points n_real_points41
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.911; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.874

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

8. Citations (1)

9. Files and Curves (10)