7w52

Crystal structure of fragmin domain-1 (15-160) in complex with actin

Method: X-RAY DIFFRACTION Dmax: 160.9 Å Quality: REASONABLE

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 × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 1–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Actin-binding protein fragmin P × 1 (Q94707) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 3 ACT ACETATE ION × 3 NA SODIUM ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium acetate, pH 4.5, 0.1 M calcium acetate, and 7% PEG3350 Resolution 2.00 Å R-free 0.246
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 1–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Actin-binding protein fragmin P × 1 (Q94707) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 3 ACT ACETATE ION × 1 NA SODIUM ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium acetate, pH 4.5, 0.1 M calcium acetate, and 7% PEG3350 Resolution 2.00 Å R-free 0.246
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain E; UniProt 1–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Actin-binding protein fragmin P × 1 (Q94707) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 3 NA SODIUM ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium acetate, pH 4.5, 0.1 M calcium acetate, and 7% PEG3350 Resolution 2.00 Å R-free 0.246
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain G; UniProt 1–377 Non-standard monomer:Yes (specific site not provided by mmCIF) Actin-binding protein fragmin P × 1 (Q94707) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 3 NA SODIUM ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium acetate, pH 4.5, 0.1 M calcium acetate, and 7% PEG3350 Resolution 2.00 Å R-free 0.246

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 63 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 C; PDBConstruct 1–377; UniProt 1–377 Author chain E; PDBConstruct 1–377; UniProt 1–377 Author chain G; PDBConstruct 1–377; UniProt 1–377

Actin-binding protein fragmin P

Physarum polycephalum

UniProt Q94707

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 15–160 Not recorded Actin, alpha skeletal muscle × 1 (P68139) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 3 ACT ACETATE ION × 3 NA SODIUM ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium acetate, pH 4.5, 0.1 M calcium acetate, and 7% PEG3350 Resolution 2.00 Å R-free 0.246
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 15–160 Not recorded Actin, alpha skeletal muscle × 1 (P68139) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 3 ACT ACETATE ION × 1 NA SODIUM ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium acetate, pH 4.5, 0.1 M calcium acetate, and 7% PEG3350 Resolution 2.00 Å R-free 0.246
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 15–160 Not recorded Actin, alpha skeletal muscle × 1 (P68139) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 3 NA SODIUM ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium acetate, pH 4.5, 0.1 M calcium acetate, and 7% PEG3350 Resolution 2.00 Å R-free 0.246
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 15–160 Not recorded Actin, alpha skeletal muscle × 1 (P68139) ATP ADENOSINE-5'-TRIPHOSPHATE × 1 CA CALCIUM ION × 3 NA SODIUM ION × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium acetate, pH 4.5, 0.1 M calcium acetate, and 7% PEG3350 Resolution 2.00 Å R-free 0.246

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.

15 other PDB entries and 18 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name Q94707_PHYPO
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 3–148; UniProt 15–160 Author chain D; PDBConstruct 3–148; UniProt 15–160 Author chain F; PDBConstruct 3–148; UniProt 15–160 Author chain H; PDBConstruct 3–148; UniProt 15–160

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 7w52

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 7w52
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2. Structure Basics 2. Structure Basics

Entry ID entry_id7w52
Deposition date deposition_date2021-11-29
Structure title titleCrystal structure of fragmin domain-1 (15-160) in complex with actin
Keywords keywordsactin dynamics, fragmin, gelsolin, ATP hydrolysis, CONTRACTILE PROTEIN; CONTRACTILE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier48.72
Radius of gyration Rg (electron density) rg_electron48.66
Forward intensity I(0) i0721881000.00
Molecular weight molecular_weight223640.0 kDa
Excluded volume excluded_volume279850 ų
Envelope volume envelope_volume403950 ų
Hydration-shell volume shell_volume70291 ų
Envelope diameter envelope_diameter159.2
Shell Rg shell_rg51.90
Envelope Rg envelope_rg47.20
Shape Rg shape_rg48.66
Total Rg total_rg48.78
Total atoms total_atoms15714
Residues n_residues1964
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 dmax160.9
Rg (real space) rg_real48.72
Rg uncertainty (real space) rg_real_error1.70
I(0) (real space) i0_real7.2190e+08
I(0) uncertainty (real space) i0_real_error1.1800e+07
Rg (reciprocal space) rg_reciprocal48.72
I(0) (reciprocal space) i0_reciprocal721900000.0000
Solution quality estimate total_estimate0.6677
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary55.3
Skewness Skewness skewness0.223
Kurtosis Kurtosis kurtosis-0.638
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha31910000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.937; Stabil: 1.000; Sysdev: 0.013; Positv: 1.000; Valcen: 0.988; Smooth: 0.839

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (8)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id7w52B01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology20 — Severin
Homologous superfamily homologous superfamily10 — Severin
Domain ID domain_id7w52D01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology20 — Severin
Homologous superfamily homologous superfamily10 — Severin
Domain ID domain_id7w52F01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology20 — Severin
Homologous superfamily homologous superfamily10 — Severin
Domain ID domain_id7w52H01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology20 — Severin
Homologous superfamily homologous superfamily10 — Severin

8. Citations (1)

9. Files and Curves (10)