9b0k

INF2 in the Middle of F-Actin (Down state)

Method: ELECTRON MICROSCOPY Dmax: 191.7 Å Quality: REASONABLE

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

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 7–377 Chain B; UniProt 7–377 Chain C; UniProt 7–377 Chain D; UniProt 7–377 Chain E; UniProt 7–377 Chain F; UniProt 7–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Inverted formin-2 × 2 (Q27J81) ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.03 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–371; UniProt 7–377 Author chain B; PDBConstruct 1–371; UniProt 7–377 Author chain C; PDBConstruct 1–371; UniProt 7–377 Author chain D; PDBConstruct 1–371; UniProt 7–377 Author chain E; PDBConstruct 1–371; UniProt 7–377 Author chain F; PDBConstruct 1–371; UniProt 7–377

Inverted formin-2

Homo sapiens

UniProt Q27J81

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 G; UniProt 551–987 Chain H; UniProt 551–987 Not recorded Actin, alpha skeletal muscle × 6 (P68135) ADP ADENOSINE-5'-DIPHOSPHATE × 6 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 8 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.03 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.

9 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name INF2_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain G; PDBConstruct 1–437; UniProt 551–987 Author chain H; PDBConstruct 1–437; UniProt 551–987

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 9b0k

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9b0k
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9b0k
Deposition date deposition_date2024-03-12
Structure title titleINF2 in the Middle of F-Actin (Down state)
Keywords keywordsActin, Formin, Filament, Severing, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier53.66
Radius of gyration Rg (electron density) rg_electron53.67
Forward intensity I(0) i01686390000.00
Molecular weight molecular_weight340790.0 kDa
Excluded volume excluded_volume425880 ų
Envelope volume envelope_volume609520 ų
Hydration-shell volume shell_volume96966 ų
Envelope diameter envelope_diameter210.5
Shell Rg shell_rg55.12
Envelope Rg envelope_rg52.70
Shape Rg shape_rg53.68
Total Rg total_rg53.66
Total atoms total_atoms23896
Residues n_residues3014
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 dmax191.7
Rg (real space) rg_real53.81
Rg uncertainty (real space) rg_real_error2.28
I(0) (real space) i0_real1.6860e+09
I(0) uncertainty (real space) i0_real_error3.3590e+07
Rg (reciprocal space) rg_reciprocal53.54
I(0) (reciprocal space) i0_reciprocal1686000000.0000
Solution quality estimate total_estimate0.6171
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary185.0
Skewness Skewness skewness0.514
Kurtosis Kurtosis kurtosis0.129
Angular range angular_range— – 0.1450 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha116900000.0000
Real-space data points n_real_points30
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.726; Stabil: 1.000; Sysdev: 0.017; Positv: 1.000; Valcen: 1.000; Smooth: 0.786

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)