6anu

Cryo-EM structure of F-actin complexed with the beta-III-spectrin actin-binding domain

Method: ELECTRON MICROSCOPY Dmax: 204.8 Å Quality: REASONABLE

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

Actin, cytoplasmic 1

Homo sapiens

UniProt P60709

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain A; UniProt 1–375 Chain B; UniProt 1–375 Chain C; UniProt 1–375 Chain D; UniProt 1–375 Chain E; UniProt 1–375 Chain F; UniProt 1–375 Not recorded Spectrin beta chain, non-erythrocytic 2 × 6 (O15020) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.00 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.

72 other PDB entries and 83 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name ACTB_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–375; UniProt 1–375 Author chain B; PDBConstruct 1–375; UniProt 1–375 Author chain C; PDBConstruct 1–375; UniProt 1–375 Author chain D; PDBConstruct 1–375; UniProt 1–375 Author chain E; PDBConstruct 1–375; UniProt 1–375 Author chain F; PDBConstruct 1–375; UniProt 1–375

Spectrin beta chain, non-erythrocytic 2

Homo sapiens

UniProt O15020

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 × 12 PDB declaration: dodecameric(12) Consistent with protein copy count Chain a; UniProt 1–284 Chain b; UniProt 1–284 Chain c; UniProt 1–284 Chain d; UniProt 1–284 Chain e; UniProt 1–284 Chain f; UniProt 1–284 Mutation:L253P Actin, cytoplasmic 1 × 6 (P60709) ELECTRON MICROSCOPY cryo-EM buffer:pH 7.4 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 7.00 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.

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SPTN2_HUMAN
Isoform O15020-2
PDB entities 2
Chains and sequence ranges Author chain a; PDBConstruct 1–284; UniProt 1–284 Author chain b; PDBConstruct 1–284; UniProt 1–284 Author chain c; PDBConstruct 1–284; UniProt 1–284 Author chain d; PDBConstruct 1–284; UniProt 1–284 Author chain e; PDBConstruct 1–284; UniProt 1–284 Author chain f; PDBConstruct 1–284; UniProt 1–284

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 6anu

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6anu
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6anu
Deposition date deposition_date2017-08-14
Structure title titleCryo-EM structure of F-actin complexed with the beta-III-spectrin actin-binding domain
Keywords keywordsactin binding protein, filament, STRUCTURAL PROTEIN; STRUCTURAL PROTEIN
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier56.36
Radius of gyration Rg (electron density) rg_electron56.98
Forward intensity I(0) i01686880000.00
Molecular weight molecular_weight342270.0 kDa
Excluded volume excluded_volume428070 ų
Envelope volume envelope_volume562360 ų
Hydration-shell volume shell_volume86587 ų
Envelope diameter envelope_diameter213.9
Shell Rg shell_rg54.01
Envelope Rg envelope_rg56.90
Shape Rg shape_rg56.98
Total Rg total_rg56.89
Total atoms total_atoms24012
Residues n_residues3048
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 dmax204.8
Rg (real space) rg_real56.84
Rg uncertainty (real space) rg_real_error1.97
I(0) (real space) i0_real1.6870e+09
I(0) uncertainty (real space) i0_real_error3.4140e+07
Rg (reciprocal space) rg_reciprocal55.95
I(0) (reciprocal space) i0_reciprocal1685000000.0000
Solution quality estimate total_estimate0.5993
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary51.2
Skewness Skewness skewness0.579
Kurtosis Kurtosis kurtosis-0.141
Angular range angular_range— – 0.1400 −1
Current regularization parameter α current_alpha0.0010
Highest regularization parameter α highest_alpha107700000.0000
Real-space data points n_real_points29
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.689; Stabil: 1.000; Sysdev: 0.041; Positv: 1.000; Valcen: 0.882; Smooth: 0.714

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)