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8v2z

Cryo-EM Structure of Smooth Muscle Gamma Actin (ACTG2) Mutant R257C

Method: ELECTRON MICROSCOPY Dmax: 173.8 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Actin, gamma-enteric smooth muscle

Homo sapiens

UniProt P63267

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 homooligomer Homooligomer Protein × 5 PDB declaration: pentameric（5） Consistent with protein copy count Chain A； UniProt 1–376 Chain B； UniProt 1–376 Chain C； UniProt 1–376 Chain D； UniProt 1–376 Chain E； UniProt 1–376 Mutation：R257C Non-standard monomer：Yes (specific site not provided by mmCIF) ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY cryo-EM buffer：pH 8；Actin F-buffer cryo-EM vitrification conditions：Cryogen ETHANE；Blot Force: 0 Blot Time: 2.5 s Resolution 2.72 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.

Other PDB Difference from Current Entry 8V2Z Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
6JAT Crystal structure of SETD3 bound to Actin peptide and SFG Deposited 2019-01-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 61–82（22 aa） Fragment：Actin peptide
Not recorded SFG SINEFUNGIN × 1 SO4 SULFATE ION × 3 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.2 M HEPES/Sodium hydroxide, 0.2 M Ammonium sulfate, 20% PEG 8000, 10% 2-propanol
Resolution 2.71 Å R-free 0.243
6JAT Crystal structure of SETD3 bound to Actin peptide and SFG Deposited 2019-01-25 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain D 61–82（22 aa） Fragment：Actin peptide
Not recorded SFG SINEFUNGIN × 1 SO4 SULFATE ION × 2 EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP；pH 7.5；291 K；0.2 M HEPES/Sodium hydroxide, 0.2 M Ammonium sulfate, 20% PEG 8000, 10% 2-propanol
Resolution 2.71 Å R-free 0.243
8V2O Cryo-EM Structure of Wildtype Smooth Muscle Gamma Actin (ACTG2) Deposited 2023-11-23 Different mutation/modification Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 5 PDB declaration: pentameric
Chain A 1–376（376 aa）
Chain B 1–376（376 aa）
Chain C 1–376（376 aa）
Chain D 1–376（376 aa）
Chain E 1–376（376 aa）
Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) Non-standard monomer：Yes (specific site not provided by mmCIF) ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 8；Actin F-buffer
cryo-EM vitrification conditions Cryogen ETHANE；Blot Force: 0 Blot Time: 2.5 s
Resolution 2.45 Å
8V30 Smooth Muscle Gamma Actin (ACTG2) Filament Mutant R40C Deposited 2023-11-25 Different mutation/modification Different oligomeric state Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 10 PDB declaration: decameric
Chain A 1–376（376 aa）
Chain B 1–376（376 aa）
Chain C 1–376（376 aa）
Chain D 1–376（376 aa）
Chain E 1–376（376 aa）
Mutation：R40C Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R40C Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R40C Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R40C Non-standard monomer：Yes (specific site not provided by mmCIF) Mutation：R40C Non-standard monomer：Yes (specific site not provided by mmCIF) ADP ADENOSINE-5'-DIPHOSPHATE × 5 MG MAGNESIUM ION × 5 ELECTRON MICROSCOPY
cryo-EM buffer pH 8；Actin F-buffer
cryo-EM vitrification conditions Cryogen ETHANE；Blot Force: 0 Blot Time: 2.5 s
Resolution 2.54 Å

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTH_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–376； UniProt 1–376 Author chain B； PDBConstruct 1–376； UniProt 1–376 Author chain C； PDBConstruct 1–376； UniProt 1–376 Author chain D； PDBConstruct 1–376； UniProt 1–376 Author chain E； PDBConstruct 1–376； UniProt 1–376

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 8v2z

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8v2z
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8v2z
Deposition date deposition_date2023-11-25
Structure title titleCryo-EM Structure of Smooth Muscle Gamma Actin (ACTG2) Mutant R257C
Keywords keywordsFilament, Actin, Smooth Muscle, CYTOSOLIC PROTEIN, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier46.70 Å
Radius of gyration Rg (electron density) rg_electron47.25 Å
Forward intensity I(0) i0654799000.00
Molecular weight molecular_weight208930.0 kDa
Excluded volume excluded_volume260420 ų
Envelope volume envelope_volume345270 ų
Hydration-shell volume shell_volume64544 ų
Envelope diameter envelope_diameter186.9 Å
Shell Rg shell_rg47.35 Å
Envelope Rg envelope_rg47.39 Å
Shape Rg shape_rg47.27 Å
Total Rg total_rg47.22 Å
Total atoms total_atoms14635
Residues n_residues1855
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax173.8 Å
Rg (real space) rg_real47.23 Å
Rg uncertainty (real space) rg_real_error2.44 Å
I(0) (real space) i0_real6.5480e+08
I(0) uncertainty (real space) i0_real_error1.2110e+07
Rg (reciprocal space) rg_reciprocal46.70 Å
I(0) (reciprocal space) i0_reciprocal654400000.0000
Solution quality estimate total_estimate0.7422
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary46.0 Å
Skewness Skewness skewness0.618
Kurtosis Kurtosis kurtosis-0.099
Angular range angular_range— – 0.1700 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha62890000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.584; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.895; Smooth: 0.000
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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8. Citations (1)

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9. Files and Curves (10)