6yp9

Rabbit muscle actin in complex with ADF-H and ATP-ATTO-488

Method: X-RAY DIFFRACTION Dmax: 82.5 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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 3–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Twinfilin-1 × 1 (Q91YR1) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;0.1 M sodium cacodylate (pH 6.0) and 15% (w/v) PEG 4000 Resolution 2.56 Å R-free 0.230

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 1–375; UniProt 3–377

Twinfilin-1

Mus musculus

UniProt Q91YR1

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain B; UniProt 176–315 Not recorded Actin, alpha skeletal muscle × 1 (P68135) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6;293 K;0.1 M sodium cacodylate (pH 6.0) and 15% (w/v) PEG 4000 Resolution 2.56 Å R-free 0.230

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.

10 other PDB entries and 11 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TWF1_MOUSE
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–140; UniProt 176–315

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 6yp9

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6yp9
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6yp9
Deposition date deposition_date2020-04-15
Structure title titleRabbit muscle actin in complex with ADF-H and ATP-ATTO-488
Keywords keywordsactin, ADF-H domain, ATP-ATTO-488, PROTEIN BINDING; PROTEIN BINDING
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.56
Radius of gyration Rg (electron density) rg_electron24.64
Forward intensity I(0) i054383600.00
Molecular weight molecular_weight57220.0 kDa
Excluded volume excluded_volume71516 ų
Envelope volume envelope_volume84074 ų
Hydration-shell volume shell_volume28529 ų
Envelope diameter envelope_diameter84.6
Shell Rg shell_rg32.06
Envelope Rg envelope_rg25.01
Shape Rg shape_rg24.67
Total Rg total_rg25.34
Total atoms total_atoms4015
Residues n_residues501
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 dmax82.5
Rg (real space) rg_real25.54
Rg uncertainty (real space) rg_real_error0.51
I(0) (real space) i0_real5.4380e+07
I(0) uncertainty (real space) i0_real_error7.1420e+05
Rg (reciprocal space) rg_reciprocal25.54
I(0) (reciprocal space) i0_reciprocal54380000.0000
Solution quality estimate total_estimate0.8969
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.9
Skewness Skewness skewness0.333
Kurtosis Kurtosis kurtosis-0.359
Angular range angular_range— – 0.3100 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha15100000.0000
Real-space data points n_real_points63
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.902; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.951

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (5)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (3 domains)

Domain ID domain_idd6yp9a1
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.1 — Actin-like ATPase domain
Family Family familyc.55.1.1 — Actin/HSP70
Domain ID domain_idd6yp9a2
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.55 — Ribonuclease H-like motif
Superfamily Superfamily superfamilyc.55.1 — Actin-like ATPase domain
Family Family familyc.55.1.1 — Actin/HSP70
Domain ID domain_idd6yp9b_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.109 — Gelsolin-like
Superfamily Superfamily superfamilyd.109.1 — Actin depolymerizing proteins
Family Family familyd.109.1.0 — automated matches

8. Citations (1)

9. Files and Curves (10)