8gt3

Crystal structure of human cardiac alpha actin P109A mutant (ADP-Pi state) in complex with fragmin F1 domain

Method: X-RAY DIFFRACTION Dmax: 85.8 Å Quality: GOOD

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

Actin, alpha cardiac muscle 1

Homo sapiens

UniProt P68032

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 3–377 Mutation:P109A Non-standard monomer:Yes (specific site not provided by mmCIF) Actin-binding protein fragmin P × 1 (Q94707) ADP ADENOSINE-5'-DIPHOSPHATE × 1 PO4 PHOSPHATE ION × 3 MG MAGNESIUM ION × 1 EDO 1,2-ETHANEDIOL × 4 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;PEG3350, Disodium Hydrogenphosphate, HEPES Resolution 1.50 Å R-free 0.196

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.

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

View Construct and Data Evidence
UniProt name ACTC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 17–391; UniProt 3–377

Actin-binding protein fragmin P

Physarum polycephalum

UniProt Q94707

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 1–160 Not recorded Actin, alpha cardiac muscle 1 × 1 (P68032) ADP ADENOSINE-5'-DIPHOSPHATE × 1 PO4 PHOSPHATE ION × 3 MG MAGNESIUM ION × 1 EDO 1,2-ETHANEDIOL × 4 CA CALCIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 8;293 K;PEG3350, Disodium Hydrogenphosphate, HEPES Resolution 1.50 Å R-free 0.196

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.

15 other PDB entries and 21 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q94707_PHYPO
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–162; UniProt 1–160

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 8gt3

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8gt3
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id8gt3
Deposition date deposition_date2022-09-07
Structure title titleCrystal structure of human cardiac alpha actin P109A mutant (ADP-Pi state) in complex with fragmin F1 domain
Keywords keywordsactin dynamics, ATP hydrolysis, mutagenesis, MD simulation, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.14
Radius of gyration Rg (electron density) rg_electron24.16
Forward intensity I(0) i057608200.00
Molecular weight molecular_weight58609.0 kDa
Excluded volume excluded_volume73024 ų
Envelope volume envelope_volume85881 ų
Hydration-shell volume shell_volume29271 ų
Envelope diameter envelope_diameter88.9
Shell Rg shell_rg32.00
Envelope Rg envelope_rg24.72
Shape Rg shape_rg24.18
Total Rg total_rg24.96
Total atoms total_atoms4118
Residues n_residues517
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 dmax85.8
Rg (real space) rg_real25.11
Rg uncertainty (real space) rg_real_error0.59
I(0) (real space) i0_real5.7610e+07
I(0) uncertainty (real space) i0_real_error8.1950e+05
Rg (reciprocal space) rg_reciprocal25.12
I(0) (reciprocal space) i0_reciprocal57610000.0000
Solution quality estimate total_estimate0.8752
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.6
Skewness Skewness skewness0.348
Kurtosis Kurtosis kurtosis-0.231
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha14970000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.803; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.970; Smooth: 0.994

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

8. Citations (1)

9. Files and Curves (10)