8syf

Homology model of Acto-HMM complex in ADP-state. Chicken smooth muscle HMM and chicken pectoralis actin

Method: ELECTRON MICROSCOPY Dmax: 206.0 Å Quality: GOOD

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

Myosin, heavy chain 11, smooth muscle

Gallus gallus

UniProt A0A8V0ZE13

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 2–844 Chain B; UniProt 2–844 Not recorded Actin, alpha skeletal muscle × 2 (P68139) Myosin light polypeptide 6 × 2 (P02607) Myosin regulatory light chain 2, smooth muscle major isoform × 2 (P02612) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 19.00 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 A0A8V0ZE13_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–843; UniProt 2–844 Author chain B; PDBConstruct 1–843; UniProt 2–844

Actin, alpha skeletal muscle

OrganismNot specified

UniProt P68139

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 3–377 Chain D; UniProt 3–377 Not recorded Myosin, heavy chain 11, smooth muscle × 2 (A0A8V0ZE13) Myosin light polypeptide 6 × 2 (P02607) Myosin regulatory light chain 2, smooth muscle major isoform × 2 (P02612) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 19.00 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.

57 other PDB entries and 66 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTS_CHICK
Isoform
PDB entities 2
Chains and sequence ranges Author chain C; PDBConstruct 1–375; UniProt 3–377 Author chain D; PDBConstruct 1–375; UniProt 3–377

Myosin light polypeptide 6

Gallus gallus

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 E; UniProt 4–151 Chain H; UniProt 4–151 Not recorded Myosin, heavy chain 11, smooth muscle × 2 (A0A8V0ZE13) Actin, alpha skeletal muscle × 2 (P68139) Myosin regulatory light chain 2, smooth muscle major isoform × 2 (P02612) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 19.00 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 3
Chains and sequence ranges Author chain E; PDBConstruct 1–148; UniProt 4–151 Author chain H; PDBConstruct 1–148; UniProt 4–151

Myosin regulatory light chain 2, smooth muscle major isoform

Gallus gallus

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 F; UniProt 26–168 Chain G; UniProt 26–168 Not recorded Myosin, heavy chain 11, smooth muscle × 2 (A0A8V0ZE13) Actin, alpha skeletal muscle × 2 (P68139) Myosin light polypeptide 6 × 2 (P02607) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.6 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 19.00 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 4
Chains and sequence ranges Author chain F; PDBConstruct 1–143; UniProt 26–168 Author chain G; PDBConstruct 1–143; UniProt 26–168

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 8syf

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8syf
Deposition date deposition_date2023-05-25
Structure title titleHomology model of Acto-HMM complex in ADP-state. Chicken smooth muscle HMM and chicken pectoralis actin
Keywords keywordsActin, Myosin, Smooth muscle, Cryo-EM, Cryo-ET, Heavy meromyosin, MOTOR PROTEIN; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier61.46
Radius of gyration Rg (electron density) rg_electron61.73
Forward intensity I(0) i01568980000.00
Molecular weight molecular_weight333870.0 kDa
Excluded volume excluded_volume417860 ų
Envelope volume envelope_volume573390 ų
Hydration-shell volume shell_volume79549 ų
Envelope diameter envelope_diameter223.0
Shell Rg shell_rg61.23
Envelope Rg envelope_rg61.26
Shape Rg shape_rg61.71
Total Rg total_rg61.77
Total atoms total_atoms23456
Residues n_residues2932
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 dmax206.0
Rg (real space) rg_real61.99
Rg uncertainty (real space) rg_real_error1.88
I(0) (real space) i0_real1.5690e+09
I(0) uncertainty (real space) i0_real_error3.2320e+07
Rg (reciprocal space) rg_reciprocal60.99
I(0) (reciprocal space) i0_reciprocal1566000000.0000
Solution quality estimate total_estimate0.8243
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary71.3
Skewness Skewness skewness0.519
Kurtosis Kurtosis kurtosis-0.068
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0005
Highest regularization parameter α highest_alpha27010000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.775; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; Smooth: 0.389

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)