7ds8

Crystal structure of actin capping protein in complex with twinflin-1/CD2AP CPI chimera peptide (CDN-TWC)

Method: X-RAY DIFFRACTION Dmax: 92.6 Å Quality: GOOD

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

F-actin-capping protein subunit alpha-1

Gallus gallus

UniProt P13127

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain A; UniProt 1–286 Not recorded F-actin-capping protein subunit beta isoforms 1 × 1 (P14315) CD2-associated protein,Twinfilin-1 × 1 (Q9Y5K6,Q91YR1) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;4% (w/v) PEG 3350, 50mM Tris-HCl (pH = 7.0) Resolution 1.95 Å R-free 0.233

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.

19 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAZA1_CHICK
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–286; UniProt 1–286

F-actin-capping protein subunit beta isoforms 1

Gallus gallus

UniProt P14315

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain B; UniProt 1–244 Not recorded F-actin-capping protein subunit alpha-1 × 1 (P13127) CD2-associated protein,Twinfilin-1 × 1 (Q9Y5K6,Q91YR1) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;4% (w/v) PEG 3350, 50mM Tris-HCl (pH = 7.0) Resolution 1.95 Å R-free 0.233

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.

19 other PDB entries and 35 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CAPZB_CHICK
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–244; UniProt 1–244

CD2-associated protein,Twinfilin-1

OrganismNot specified

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 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 326–344 Not recorded F-actin-capping protein subunit alpha-1 × 1 (P13127) F-actin-capping protein subunit beta isoforms 1 × 1 (P14315) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;4% (w/v) PEG 3350, 50mM Tris-HCl (pH = 7.0) Resolution 1.95 Å R-free 0.233

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 3
Chains and sequence ranges Author chain C; PDBConstruct 10–28; UniProt 326–344

CD2-associated protein,Twinfilin-1

OrganismNot specified

UniProt Q9Y5K6

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Heteromer Protein × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 485–493 Not recorded F-actin-capping protein subunit alpha-1 × 1 (P13127) F-actin-capping protein subunit beta isoforms 1 × 1 (P14315) X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;4% (w/v) PEG 3350, 50mM Tris-HCl (pH = 7.0) Resolution 1.95 Å R-free 0.233

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.

11 other PDB entries and 36 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name CD2AP_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 1–9; UniProt 485–493

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 7ds8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7ds8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7ds8
Deposition date deposition_date2020-12-30
Structure title titleCrystal structure of actin capping protein in complex with twinflin-1/CD2AP CPI chimera peptide (CDN-TWC)
Keywords keywordsactin dynamics, actin capping protein, twinfilin, CARMIL, V-1, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier27.88
Radius of gyration Rg (electron density) rg_electron27.09
Forward intensity I(0) i060602400.00
Molecular weight molecular_weight59385.0 kDa
Excluded volume excluded_volume73684 ų
Envelope volume envelope_volume90197 ų
Hydration-shell volume shell_volume28575 ų
Envelope diameter envelope_diameter95.5
Shell Rg shell_rg33.64
Envelope Rg envelope_rg27.38
Shape Rg shape_rg27.09
Total Rg total_rg27.75
Total atoms total_atoms4187
Residues n_residues528
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 dmax92.6
Rg (real space) rg_real28.01
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real6.0600e+07
I(0) uncertainty (real space) i0_real_error9.4400e+05
Rg (reciprocal space) rg_reciprocal27.97
I(0) (reciprocal space) i0_reciprocal60600000.0000
Solution quality estimate total_estimate0.8770
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary29.2
Skewness Skewness skewness0.455
Kurtosis Kurtosis kurtosis-0.322
Angular range angular_range— – 0.2850 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha20370000.0000
Real-space data points n_real_points58
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.855; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.937; Smooth: 0.896

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)