9az4

INF2 at the Barbed End of F-Actin

Method: ELECTRON MICROSCOPY Dmax: 224.7 Å Quality: GOOD

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 3.37 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 3.37 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 9az4

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9az4
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9az4
Deposition date deposition_date2024-03-10
Structure title titleINF2 at the Barbed End of F-Actin
Keywords keywordsActin, Filament, Elongation, Ends, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier61.49
Radius of gyration Rg (electron density) rg_electron62.34
Forward intensity I(0) i01669330000.00
Molecular weight molecular_weight340350.0 kDa
Excluded volume excluded_volume425340 ų
Envelope volume envelope_volume622800 ų
Hydration-shell volume shell_volume89456 ų
Envelope diameter envelope_diameter222.6
Shell Rg shell_rg55.56
Envelope Rg envelope_rg61.98
Shape Rg shape_rg62.36
Total Rg total_rg62.11
Total atoms total_atoms23865
Residues n_residues3009
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 dmax224.7
Rg (real space) rg_real62.25
Rg uncertainty (real space) rg_real_error2.88
I(0) (real space) i0_real1.6690e+09
I(0) uncertainty (real space) i0_real_error3.8890e+07
Rg (reciprocal space) rg_reciprocal60.81
I(0) (reciprocal space) i0_reciprocal1665000000.0000
Solution quality estimate total_estimate0.8043
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.9
Skewness Skewness skewness0.568
Kurtosis Kurtosis kurtosis-0.345
Angular range angular_range— – 0.1300 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha114600000.0000
Real-space data points n_real_points27
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.622; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.939; Smooth: 0.646

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)