7dsa

Crystal structure of actin capping protein in complex with V-1 (space group P62)

Method: X-RAY DIFFRACTION Dmax: 91.4 Å Quality: REASONABLE

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 Protein heterocomplex 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) Myotrophin × 1 (P58546) MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;20% (w/v) PEG 3350, 0.2M Magnesium Acetate Resolution 2.80 Å R-free 0.254

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 Protein heterocomplex 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) Myotrophin × 1 (P58546) MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;20% (w/v) PEG 3350, 0.2M Magnesium Acetate Resolution 2.80 Å R-free 0.254

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

Myotrophin

Homo sapiens

UniProt P58546

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 × 3 PDB declaration: trimeric(3) Consistent with protein copy count Chain C; UniProt 1–118 Not recorded F-actin-capping protein subunit alpha-1 × 1 (P13127) F-actin-capping protein subunit beta isoforms 1 × 1 (P14315) MG MAGNESIUM ION × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;20% (w/v) PEG 3350, 0.2M Magnesium Acetate Resolution 2.80 Å R-free 0.254

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.

3 other PDB entries and 4 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MTPN_HUMAN
Isoform
PDB entities 3
Chains and sequence ranges Author chain C; PDBConstruct 6–123; UniProt 1–118

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 7dsa

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7dsa
Deposition date deposition_date2020-12-30
Structure title titleCrystal structure of actin capping protein in complex with V-1 (space group P62)
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_guinier29.29
Radius of gyration Rg (electron density) rg_electron28.47
Forward intensity I(0) i080290700.00
Molecular weight molecular_weight69085.0 kDa
Excluded volume excluded_volume85890 ų
Envelope volume envelope_volume107650 ų
Hydration-shell volume shell_volume31887 ų
Envelope diameter envelope_diameter97.9
Shell Rg shell_rg35.28
Envelope Rg envelope_rg28.61
Shape Rg shape_rg28.47
Total Rg total_rg29.13
Total atoms total_atoms4867
Residues n_residues620
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 dmax91.4
Rg (real space) rg_real29.29
Rg uncertainty (real space) rg_real_error0.63
I(0) (real space) i0_real8.0290e+07
I(0) uncertainty (real space) i0_real_error1.1540e+06
Rg (reciprocal space) rg_reciprocal29.29
I(0) (reciprocal space) i0_reciprocal80290000.0000
Solution quality estimate total_estimate0.6884
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary33.9
Skewness Skewness skewness0.294
Kurtosis Kurtosis kurtosis-0.515
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha27590000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.959; Stabil: 1.000; Sysdev: 0.092; Positv: 1.000; Valcen: 0.994; Smooth: 0.796

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_idd7dsaa_
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.43 — Subunits of heterodimeric actin filament capping protein Capz
Superfamily Superfamily superfamilye.43.1 — Subunits of heterodimeric actin filament capping protein Capz
Family Family familye.43.1.1 — Capz alpha-1 subunit
Domain ID domain_idd7dsab_
Class classe — Multi-domain proteins (alpha and beta)
Fold Fold folde.43 — Subunits of heterodimeric actin filament capping protein Capz
Superfamily Superfamily superfamilye.43.1 — Subunits of heterodimeric actin filament capping protein Capz
Family Family familye.43.1.2 — Capz beta-1 subunit
Domain ID domain_idd7dsac_
Class classd — Alpha and beta proteins (a+b)
Fold Fold foldd.211 — beta-hairpin-alpha-hairpin repeat
Superfamily Superfamily superfamilyd.211.1 — Ankyrin repeat
Family Family familyd.211.1.1 — Ankyrin repeat

8. Citations (1)

9. Files and Curves (10)