8enc

Helical reconstruction of the human cardiac actin-tropomyosin-myosin loop 4 7G mutant complex

Method: ELECTRON MICROSCOPY Dmax: 227.8 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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain M; UniProt 1–1935 Mutation:Residues 366-372 substituted with seven glycines Actin, alpha cardiac muscle 1 × 5 (B6VNT8) Tropomyosin alpha-1 chain × 2 (P09493) ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 M; PDBConstruct 1–1935; UniProt 1–1935

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain B; UniProt 1–377 Chain C; UniProt 1–377 Chain D; UniProt 1–377 Chain E; UniProt 1–377 Chain F; UniProt 1–377 Not recorded Myosin-7 × 1 (P12883) Tropomyosin alpha-1 chain × 2 (P09493) ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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 2
Chains and sequence ranges Author chain B; PDBConstruct 1–377; UniProt 1–377 Author chain C; PDBConstruct 1–377; UniProt 1–377 Author chain D; PDBConstruct 1–377; UniProt 1–377 Author chain E; PDBConstruct 1–377; UniProt 1–377 Author chain F; PDBConstruct 1–377; UniProt 1–377

Tropomyosin alpha-1 chain

Homo sapiens

UniProt P09493

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain O; UniProt 1–284 Chain P; UniProt 1–284 Not recorded Myosin-7 × 1 (P12883) Actin, alpha cardiac muscle 1 × 5 (B6VNT8) ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.60 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_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain O; PDBConstruct 1–284; UniProt 1–284 Author chain P; 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 8enc

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8enc
Deposition date deposition_date2022-09-29
Structure title titleHelical reconstruction of the human cardiac actin-tropomyosin-myosin loop 4 7G mutant complex
Keywords keywordsactin, tropomyosin, myosin, cardiac, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier55.73
Radius of gyration Rg (electron density) rg_electron55.95
Forward intensity I(0) i01589260000.00
Molecular weight molecular_weight330880.0 kDa
Excluded volume excluded_volume413270 ų
Envelope volume envelope_volume611010 ų
Hydration-shell volume shell_volume93911 ų
Envelope diameter envelope_diameter247.2
Shell Rg shell_rg55.29
Envelope Rg envelope_rg56.28
Shape Rg shape_rg55.95
Total Rg total_rg55.94
Total atoms total_atoms23220
Residues n_residues2929
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 dmax227.8
Rg (real space) rg_real55.90
Rg uncertainty (real space) rg_real_error3.68
I(0) (real space) i0_real1.5890e+09
I(0) uncertainty (real space) i0_real_error3.4460e+07
Rg (reciprocal space) rg_reciprocal55.59
I(0) (reciprocal space) i0_reciprocal1589000000.0000
Solution quality estimate total_estimate0.7981
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary57.0
Skewness Skewness skewness0.435
Kurtosis Kurtosis kurtosis-0.126
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha148300000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.518; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.822; Smooth: 0.993

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id8encB01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id8encC01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id8encD01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id8encE01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id8encF01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id8encM01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily60

8. Citations (1)

9. Files and Curves (10)