7bti

Phalloidin bound F-actin complex

Method: ELECTRON MICROSCOPY Dmax: 172.9 Å Quality: GOOD

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

Actin, alpha skeletal muscle

OrganismNot specified

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 × 8 PDB declaration: octameric(8) Consistent with protein copy count Chain A; UniProt 1–377 Chain B; UniProt 1–377 Chain C; UniProt 1–377 Chain D; UniProt 1–377 Chain E; UniProt 1–377 Not recorded Phalloidin × 3 MG MAGNESIUM ION × 5 ADP ADENOSINE-5'-DIPHOSPHATE × 5 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5;50mM KCl,1mM MgCl2,0.2mM EGTA, 10mM Imidazole buffer pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE;blot for 3.5 seconds Resolution 3.60 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 1
Chains and sequence ranges Author chain A; PDBConstruct 1–377; UniProt 1–377 Author chain B; PDBConstruct 1–377; UniProt 1–377 Author chain C; PDBConstruct 1–377; UniProt 1–377 Author chain D; PDBConstruct 1–377; UniProt 1–377 Author chain E; 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 7bti

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7bti
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7bti
Deposition date deposition_date2020-04-01
Structure title titlePhalloidin bound F-actin complex
Keywords keywordsF-actin, ADP-F-actin, CONTRACTILE PROTEIN, CONTRACTILE PROTEIN-PROTEIN BINDING complex; CONTRACTILE PROTEIN/PROTEIN BINDING
Experimental Method methodELECTRON MICROSCOPY

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

Radius of gyration Rg (Guinier) rg_guinier46.84
Radius of gyration Rg (electron density) rg_electron47.44
Forward intensity I(0) i0656492000.00
Molecular weight molecular_weight209110.0 kDa
Excluded volume excluded_volume260690 ų
Envelope volume envelope_volume350440 ų
Hydration-shell volume shell_volume65457 ų
Envelope diameter envelope_diameter185.1
Shell Rg shell_rg47.32
Envelope Rg envelope_rg47.59
Shape Rg shape_rg47.46
Total Rg total_rg47.40
Total atoms total_atoms14650
Residues n_residues1851
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 dmax172.9
Rg (real space) rg_real47.40
Rg uncertainty (real space) rg_real_error2.34
I(0) (real space) i0_real6.5650e+08
I(0) uncertainty (real space) i0_real_error1.3530e+07
Rg (reciprocal space) rg_reciprocal46.84
I(0) (reciprocal space) i0_reciprocal656000000.0000
Solution quality estimate total_estimate0.8099
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary45.8
Skewness Skewness skewness0.633
Kurtosis Kurtosis kurtosis-0.073
Angular range angular_range— – 0.1700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha75410000.0000
Real-space data points n_real_points35
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.592; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.896; Smooth: 0.851

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 6 domains

CATH v4.4 (6 domains)

Domain ID domain_id7btiA01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id7btiB01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id7btiC01
Class class3 — Alpha Beta
Architecture architecture30 — 2-Layer Sandwich
Topology topology420 — Nucleotidyltransferase; domain 5
Homologous superfamily homologous superfamily40 — ATPase, nucleotide binding domain
Domain ID domain_id7btiC02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id7btiD01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4
Domain ID domain_id7btiE01
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology640 — Actin; Chain A, domain 4
Homologous superfamily homologous superfamily10 — ATPase, substrate binding domain, subdomain 4

8. Citations (1)

9. Files and Curves (10)