5h53

The structure of rabbit skeletal muscle actomyosin rigor complex at 5.2 angstrom.

Method: ELECTRON MICROSCOPY Dmax: 208.1 Å Quality: REASONABLE

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

Skeletal muscle myosin heavy chain MyHC-EO/IIL

OrganismNot specified

UniProt Q9GJP9

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain A; UniProt 1–845 Fragment:UNP residues 1-845 Myosin regulatory light chain 2, skeletal muscle isoform type 1 × 1 (P24732) Myosin light chain 1/3, skeletal muscle isoform × 1 (P02602) Actin, alpha skeletal muscle × 2 (P68135) ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.20 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name Q9GJP9_RABIT
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–845; UniProt 1–845

Myosin regulatory light chain 2, skeletal muscle isoform type 1

OrganismNot specified

UniProt P24732

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain B; UniProt 25–170 Fragment:UNP residues 25-170 Skeletal muscle myosin heavy chain MyHC-EO/IIL × 1 (Q9GJP9) Myosin light chain 1/3, skeletal muscle isoform × 1 (P02602) Actin, alpha skeletal muscle × 2 (P68135) ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.20 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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name MLRT_RABIT
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–146; UniProt 25–170

Myosin light chain 1/3, skeletal muscle isoform

OrganismNot specified

UniProt P02602

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain C; UniProt 41–192 Fragment:UNP residues 41-192 Skeletal muscle myosin heavy chain MyHC-EO/IIL × 1 (Q9GJP9) Myosin regulatory light chain 2, skeletal muscle isoform type 1 × 1 (P24732) Actin, alpha skeletal muscle × 2 (P68135) ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.20 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.

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYL1_RABIT
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–152; UniProt 41–192

Actin, alpha skeletal muscle

OrganismNot specified

UniProt P68135

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 × 5 PDB declaration: pentameric(5) Consistent with protein copy count Chain D; UniProt 3–377 Chain E; UniProt 3–377 Fragment:UNP residues 3-377 Non-standard monomer:Yes (specific site not provided by mmCIF) Skeletal muscle myosin heavy chain MyHC-EO/IIL × 1 (Q9GJP9) Myosin regulatory light chain 2, skeletal muscle isoform type 1 × 1 (P24732) Myosin light chain 1/3, skeletal muscle isoform × 1 (P02602) ADP ADENOSINE-5'-DIPHOSPHATE × 2 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 5.20 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.

293 other PDB entries and 353 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_RABIT
Isoform
PDB entities 4
Chains and sequence ranges Author chain D; PDBConstruct 1–375; UniProt 3–377 Author chain E; PDBConstruct 1–375; UniProt 3–377

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 5h53

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5h53
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5h53
Deposition date deposition_date2016-11-04
Structure title titleThe structure of rabbit skeletal muscle actomyosin rigor complex at 5.2 angstrom.
Keywords keywordsActin, Myosin, Muscle, rigor complex, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.58
Radius of gyration Rg (electron density) rg_electron57.74
Forward intensity I(0) i0670576000.00
Molecular weight molecular_weight214780.0 kDa
Excluded volume excluded_volume268660 ų
Envelope volume envelope_volume415880 ų
Hydration-shell volume shell_volume65820 ų
Envelope diameter envelope_diameter221.2
Shell Rg shell_rg52.05
Envelope Rg envelope_rg59.63
Shape Rg shape_rg57.71
Total Rg total_rg57.64
Total atoms total_atoms15077
Residues n_residues1892
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 dmax208.1
Rg (real space) rg_real57.51
Rg uncertainty (real space) rg_real_error2.76
I(0) (real space) i0_real6.7060e+08
I(0) uncertainty (real space) i0_real_error1.4280e+07
Rg (reciprocal space) rg_reciprocal55.82
I(0) (reciprocal space) i0_reciprocal668900000.0000
Solution quality estimate total_estimate0.5387
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary59.5
Skewness Skewness skewness0.751
Kurtosis Kurtosis kurtosis0.165
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha37350000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.598; Stabil: 1.000; Sysdev: 0.041; Positv: 1.000; Valcen: 0.671; Smooth: 0.410

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)