7yne

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

Method: X-RAY DIFFRACTION Dmax: 161.9 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 × 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) ADP ADENOSINE-5'-DIPHOSPHATE × 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 5.0, 0.1 M calcium acetate, and 12% PEG4000 Resolution 2.70 Å R-free 0.308
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) ADP ADENOSINE-5'-DIPHOSPHATE × 1 CA CALCIUM ION × 3 ACT ACETATE ION × 1 NA SODIUM ION × 1 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium acetate, pH 5.0, 0.1 M calcium acetate, and 12% PEG4000 Resolution 2.70 Å R-free 0.308
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) ADP ADENOSINE-5'-DIPHOSPHATE × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium acetate, pH 5.0, 0.1 M calcium acetate, and 12% PEG4000 Resolution 2.70 Å R-free 0.308
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) ADP ADENOSINE-5'-DIPHOSPHATE × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium acetate, pH 5.0, 0.1 M calcium acetate, and 12% PEG4000 Resolution 2.70 Å R-free 0.308

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 1–160 Not recorded Actin, alpha skeletal muscle × 1 (P68139) ADP ADENOSINE-5'-DIPHOSPHATE × 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 5.0, 0.1 M calcium acetate, and 12% PEG4000 Resolution 2.70 Å R-free 0.308
2 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain D; UniProt 1–160 Not recorded Actin, alpha skeletal muscle × 1 (P68139) ADP ADENOSINE-5'-DIPHOSPHATE × 1 CA CALCIUM ION × 3 ACT ACETATE ION × 1 NA SODIUM ION × 1 PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium acetate, pH 5.0, 0.1 M calcium acetate, and 12% PEG4000 Resolution 2.70 Å R-free 0.308
3 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain F; UniProt 1–160 Not recorded Actin, alpha skeletal muscle × 1 (P68139) ADP ADENOSINE-5'-DIPHOSPHATE × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium acetate, pH 5.0, 0.1 M calcium acetate, and 12% PEG4000 Resolution 2.70 Å R-free 0.308
4 Protein heterocomplex Heteromer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain H; UniProt 1–160 Not recorded Actin, alpha skeletal muscle × 1 (P68139) ADP ADENOSINE-5'-DIPHOSPHATE × 1 CA CALCIUM ION × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;0.1 M sodium acetate, pH 5.0, 0.1 M calcium acetate, and 12% PEG4000 Resolution 2.70 Å R-free 0.308

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 3–162; UniProt 1–160 Author chain D; PDBConstruct 3–162; UniProt 1–160 Author chain F; PDBConstruct 3–162; UniProt 1–160 Author chain H; PDBConstruct 3–162; UniProt 1–160

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 7yne

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id7yne
Deposition date deposition_date2022-07-30
Structure title titleCrystal structure of fragmin domain-1 (1-160) in complex with G-form 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_guinier49.00
Radius of gyration Rg (electron density) rg_electron48.94
Forward intensity I(0) i0626634000.00
Molecular weight molecular_weight205210.0 kDa
Excluded volume excluded_volume255210 ų
Envelope volume envelope_volume382580 ų
Hydration-shell volume shell_volume66910 ų
Envelope diameter envelope_diameter160.8
Shell Rg shell_rg51.53
Envelope Rg envelope_rg47.29
Shape Rg shape_rg48.95
Total Rg total_rg48.98
Total atoms total_atoms14444
Residues n_residues1920
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 dmax161.9
Rg (real space) rg_real49.03
Rg uncertainty (real space) rg_real_error1.57
I(0) (real space) i0_real6.2660e+08
I(0) uncertainty (real space) i0_real_error1.1900e+07
Rg (reciprocal space) rg_reciprocal49.00
I(0) (reciprocal space) i0_reciprocal626600000.0000
Solution quality estimate total_estimate0.8305
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary60.7
Skewness Skewness skewness0.229
Kurtosis Kurtosis kurtosis-0.634
Angular range angular_range— – 0.1600 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha26370000.0000
Real-space data points n_real_points33
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.936; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.983; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (9)

7. Fold Classification (SCOP + CATH) 4 domains

CATH v4.4 (4 domains)

Domain ID domain_id7yneB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology20 — Severin
Homologous superfamily homologous superfamily10 — Severin
Domain ID domain_id7yneD01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology20 — Severin
Homologous superfamily homologous superfamily10 — Severin
Domain ID domain_id7yneF01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology20 — Severin
Homologous superfamily homologous superfamily10 — Severin
Domain ID domain_id7yneH01
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)