7mf3

Structure of the autoinhibited state of smooth muscle myosin-2

Method: ELECTRON MICROSCOPY Dmax: 205.8 Å Quality: GOOD

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

Myosin-11

OrganismNot specified

UniProt P10587

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 A; UniProt 2–1979 Chain B; UniProt 2–1979 Chain G; UniProt 2–1979 Chain H; UniProt 2–1979 Not recorded Myosin light polypeptide 6 × 2 (P02607) Myosin regulatory light chain 2, smooth muscle major isoform × 2 (P02612) ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3;150 mM NaCl, 1mM EGTA, 2mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

8 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYH11_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–1978; UniProt 2–1979 Author chain B; PDBConstruct 1–1978; UniProt 2–1979 Author chain G; PDBConstruct 1–1978; UniProt 2–1979 Author chain H; PDBConstruct 1–1978; UniProt 2–1979

Myosin light polypeptide 6

OrganismNot specified

UniProt P02607

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 C; UniProt 2–151 Chain F; UniProt 2–151 Not recorded Myosin-11 × 4 (P10587) Myosin regulatory light chain 2, smooth muscle major isoform × 2 (P02612) ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3;150 mM NaCl, 1mM EGTA, 2mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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.

7 other PDB entries and 15 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYL6_CHICK
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–150; UniProt 2–151 Author chain F; PDBConstruct 1–150; UniProt 2–151

Myosin regulatory light chain 2, smooth muscle major isoform

OrganismNot specified

UniProt P02612

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 D; UniProt 2–172 Chain E; UniProt 2–172 Not recorded Myosin-11 × 4 (P10587) Myosin light polypeptide 6 × 2 (P02607) ADP ADENOSINE-5'-DIPHOSPHATE × 2 PO4 PHOSPHATE ION × 2 MG MAGNESIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.3;150 mM NaCl, 1mM EGTA, 2mM MgCl2 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.40 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 MLRM_CHICK
Isoform
PDB entities 3
Chains and sequence ranges Author chain D; PDBConstruct 1–171; UniProt 2–172 Author chain E; PDBConstruct 1–171; UniProt 2–172

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 7mf3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7mf3
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7mf3
Deposition date deposition_date2021-04-08
Structure title titleStructure of the autoinhibited state of smooth muscle myosin-2
Keywords keywordsMuscle contraction, ATPase, autoinhibition, 10S, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier60.70
Radius of gyration Rg (electron density) rg_electron60.72
Forward intensity I(0) i01590880000.00
Molecular weight molecular_weight326920.0 kDa
Excluded volume excluded_volume406710 ų
Envelope volume envelope_volume711070 ų
Hydration-shell volume shell_volume101050 ų
Envelope diameter envelope_diameter220.7
Shell Rg shell_rg59.27
Envelope Rg envelope_rg58.68
Shape Rg shape_rg60.70
Total Rg total_rg60.75
Total atoms total_atoms22938
Residues n_residues2822
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 dmax205.8
Rg (real space) rg_real60.77
Rg uncertainty (real space) rg_real_error2.55
I(0) (real space) i0_real1.5910e+09
I(0) uncertainty (real space) i0_real_error3.5650e+07
Rg (reciprocal space) rg_reciprocal60.61
I(0) (reciprocal space) i0_reciprocal1590000000.0000
Solution quality estimate total_estimate0.8780
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary71.2
Skewness Skewness skewness0.326
Kurtosis Kurtosis kurtosis-0.330
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha126200000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.894; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.736

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)