9qgk

F-actin decorated by ITPKA

Method: ELECTRON MICROSCOPY Dmax: 177.3 Å Quality: REASONABLE

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

Inositol-trisphosphate 3-kinase A

Homo sapiens

UniProt P23677

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 × 13 PDB declaration: 13-meric(13) Consistent with protein copy count Chain A; UniProt 1–461 Chain B; UniProt 1–461 Chain C; UniProt 1–461 Chain D; UniProt 1–461 Chain E; UniProt 1–461 Not recorded Actin, alpha skeletal muscle × 5 (P68139) Phalloidin × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.97 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.

16 other PDB entries and 32 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name IP3KA_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–461; UniProt 1–461 Author chain B; PDBConstruct 1–461; UniProt 1–461 Author chain C; PDBConstruct 1–461; UniProt 1–461 Author chain D; PDBConstruct 1–461; UniProt 1–461 Author chain E; PDBConstruct 1–461; UniProt 1–461

Actin, alpha skeletal muscle

Gallus

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 × 13 PDB declaration: 13-meric(13) Consistent with protein copy count Chain F; UniProt 1–377 Chain G; UniProt 1–377 Chain H; UniProt 1–377 Chain I; UniProt 1–377 Chain J; UniProt 1–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Inositol-trisphosphate 3-kinase A × 5 (P23677) Phalloidin × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE-PROPANE Resolution 2.97 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 F; PDBConstruct 1–377; UniProt 1–377 Author chain G; PDBConstruct 1–377; UniProt 1–377 Author chain H; PDBConstruct 1–377; UniProt 1–377 Author chain I; PDBConstruct 1–377; UniProt 1–377 Author chain J; 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 9qgk

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9qgk
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9qgk
Deposition date deposition_date2025-03-13
Structure title titleF-actin decorated by ITPKA
Keywords keywordsactin, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.98
Radius of gyration Rg (electron density) rg_electron47.50
Forward intensity I(0) i0745393000.00
Molecular weight molecular_weight223250.0 kDa
Excluded volume excluded_volume278430 ų
Envelope volume envelope_volume363460 ų
Hydration-shell volume shell_volume67139 ų
Envelope diameter envelope_diameter189.9
Shell Rg shell_rg47.78
Envelope Rg envelope_rg47.79
Shape Rg shape_rg47.51
Total Rg total_rg47.48
Total atoms total_atoms30895
Residues n_residues1977
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 dmax177.3
Rg (real space) rg_real47.51
Rg uncertainty (real space) rg_real_error2.40
I(0) (real space) i0_real7.4540e+08
I(0) uncertainty (real space) i0_real_error1.4860e+07
Rg (reciprocal space) rg_reciprocal46.98
I(0) (reciprocal space) i0_reciprocal744900000.0000
Solution quality estimate total_estimate0.5815
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary46.9
Skewness Skewness skewness0.619
Kurtosis Kurtosis kurtosis-0.074
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha96260000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.558; Stabil: 1.000; Sysdev: 0.021; Positv: 1.000; Valcen: 0.882; Smooth: 0.935

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

8. Citations (1)

9. Files and Curves (10)