9fn6

Full-length crystal structure of human Fascin 1

Method: X-RAY DIFFRACTION Dmax: 107.2 Å Quality: GOOD

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

Fascin

Homo sapiens

UniProt Q16658

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 monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 1–493 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0,1M HEPES pH 7.5, 20% polyethylene glycol (PEG) 4000, 2% propanol Resolution 2.20 Å R-free 0.304
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–493 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;293 K;0,1M HEPES pH 7.5, 20% polyethylene glycol (PEG) 4000, 2% propanol Resolution 2.20 Å R-free 0.304

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.

27 other PDB entries and 49 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FSCN1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–493; UniProt 1–493 Author chain B; PDBConstruct 1–493; UniProt 1–493

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 9fn6

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9fn6
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9fn6
Deposition date deposition_date2024-06-09
Structure title titleFull-length crystal structure of human Fascin 1
Keywords keywordsActin-binding protein, Cancer, Metastasis, 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_guinier33.82
Radius of gyration Rg (electron density) rg_electron32.85
Forward intensity I(0) i0194502000.00
Molecular weight molecular_weight107970.0 kDa
Excluded volume excluded_volume133540 ų
Envelope volume envelope_volume171150 ų
Hydration-shell volume shell_volume43225 ų
Envelope diameter envelope_diameter111.2
Shell Rg shell_rg39.96
Envelope Rg envelope_rg32.29
Shape Rg shape_rg32.82
Total Rg total_rg33.49
Total atoms total_atoms7592
Residues n_residues970
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 dmax107.2
Rg (real space) rg_real33.75
Rg uncertainty (real space) rg_real_error0.84
I(0) (real space) i0_real1.9450e+08
I(0) uncertainty (real space) i0_real_error2.9890e+06
Rg (reciprocal space) rg_reciprocal33.79
I(0) (reciprocal space) i0_reciprocal194500000.0000
Solution quality estimate total_estimate0.8993
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks0
Primary peak position r_peak_primary
Skewness Skewness skewness0.220
Kurtosis Kurtosis kurtosis-0.510
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha29950000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.945; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.854

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

8. Citations (1)

9. Files and Curves (10)