7pm1

Cryo-EM structure of the actomyosin-V complex in the rigor state (central 1er, young JASP-stabilized F-actin, class 2)

Method: ELECTRON MICROSCOPY Dmax: 158.2 Å Quality: GOOD

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

Myosin light chain 6B

Homo sapiens

UniProt P14649

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 59–208 Not recorded Unconventional myosin-Va × 1 (Q02440) Actin, alpha skeletal muscle × 1 (P68135) ADP ADENOSINE-5'-DIPHOSPHATE × 1 PO4 PHOSPHATE ION × 1 MG MAGNESIUM ION × 1 9UE Jasplakinolide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;On grid decoration Resolution 3.50 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.

28 other PDB entries and 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYL6B_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 2–151; UniProt 59–208

Unconventional myosin-Va

Gallus gallus

UniProt Q02440

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–792 Not recorded Myosin light chain 6B × 1 (P14649) Actin, alpha skeletal muscle × 1 (P68135) ADP ADENOSINE-5'-DIPHOSPHATE × 1 PO4 PHOSPHATE ION × 1 MG MAGNESIUM ION × 1 9UE Jasplakinolide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;On grid decoration Resolution 3.50 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.

30 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MYO5A_CHICK
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–792; UniProt 1–792

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Myosin light chain 6B × 1 (P14649) Unconventional myosin-Va × 1 (Q02440) ADP ADENOSINE-5'-DIPHOSPHATE × 1 PO4 PHOSPHATE ION × 1 MG MAGNESIUM ION × 1 9UE Jasplakinolide × 1 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;On grid decoration Resolution 3.50 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 3
Chains and sequence ranges Author chain C; PDBConstruct 1–377; UniProt 1–377

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 7pm1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7pm1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7pm1
Deposition date deposition_date2021-09-01
Structure title titleCryo-EM structure of the actomyosin-V complex in the rigor state (central 1er, young JASP-stabilized F-actin, class 2)
Keywords keywordsMotor protein, myosin, cytoskeleton, F-actin, jasplakinolide; MOTOR PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier44.32
Radius of gyration Rg (electron density) rg_electron44.83
Forward intensity I(0) i0309705000.00
Molecular weight molecular_weight144690.0 kDa
Excluded volume excluded_volume181550 ų
Envelope volume envelope_volume255870 ų
Hydration-shell volume shell_volume51860 ų
Envelope diameter envelope_diameter166.8
Shell Rg shell_rg44.34
Envelope Rg envelope_rg44.94
Shape Rg shape_rg44.78
Total Rg total_rg44.95
Total atoms total_atoms10169
Residues n_residues1260
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 dmax158.2
Rg (real space) rg_real44.94
Rg uncertainty (real space) rg_real_error1.92
I(0) (real space) i0_real3.0970e+08
I(0) uncertainty (real space) i0_real_error6.8190e+06
Rg (reciprocal space) rg_reciprocal44.33
I(0) (reciprocal space) i0_reciprocal309500000.0000
Solution quality estimate total_estimate0.7805
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary39.6
Skewness Skewness skewness0.673
Kurtosis Kurtosis kurtosis0.010
Angular range angular_range— – 0.1800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha40010000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.655; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.655; Smooth: 0.523

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (7)

7. Fold Classification (SCOP + CATH) 1 domains

CATH v4.4 (1 domains)

Domain ID domain_id7pm1A01
Class class1 — Mainly Alpha
Architecture architecture20 — Up-down Bundle
Topology topology58 — Methane Monooxygenase Hydroxylase; Chain G, domain 1
Homologous superfamily homologous superfamily530

8. Citations (1)

9. Files and Curves (10)