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8yq1

Linear form of FGF10 from Homo sapiens

Method: X-RAY DIFFRACTION Dmax: 65.2 Å Quality: EXCELLENT
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Fibroblast growth factor 10

Homo sapiens

UniProt O15520

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 66–207 Chain B； UniProt 66–207 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：VAPOR DIFFUSION, HANGING DROP；288 K；0.2 M Ammonium Sulfate, 10% PEG 4000, 0.1 M Tris-HCl pH 6.5 Resolution 2.56 Å R-free 0.278

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.

Other PDB Difference from Current Entry 8YQ1 Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1NUN Crystal Structure Analysis of the FGF10-FGFR2b Complex Deposited 2003-01-31 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric
Chain A 64–208（145 aa）
Not recorded SO4 SULFATE ION × 2 15P POLYETHYLENE GLYCOL (N=34) × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；PEG 400, ammonium sulfate, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Resolution 2.90 Å R-free 0.288

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FGF10_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–142； UniProt 66–207 Author chain B； PDBConstruct 1–142； UniProt 66–207

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 8yq1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8yq1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8yq1
Deposition date deposition_date2024-03-18
Structure title titleLinear form of FGF10 from Homo sapiens
Keywords keywordsGrowth Factor, FGF10, Fibroblast, HORMONE; HORMONE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier21.11 Å
Radius of gyration Rg (electron density) rg_electron20.09 Å
Forward intensity I(0) i017498300.00
Molecular weight molecular_weight31243.0 kDa
Excluded volume excluded_volume38948 ų
Envelope volume envelope_volume47037 ų
Hydration-shell volume shell_volume19906 ų
Envelope diameter envelope_diameter64.4 Å
Shell Rg shell_rg25.96 Å
Envelope Rg envelope_rg20.31 Å
Shape Rg shape_rg20.09 Å
Total Rg total_rg20.92 Å
Total atoms total_atoms2206
Residues n_residues281
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax65.2 Å
Rg (real space) rg_real21.08 Å
Rg uncertainty (real space) rg_real_error0.37 Å
I(0) (real space) i0_real1.7500e+07
I(0) uncertainty (real space) i0_real_error2.1980e+05
Rg (reciprocal space) rg_reciprocal21.09 Å
I(0) (reciprocal space) i0_reciprocal17500000.0000
Solution quality estimate total_estimate0.9050
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary23.0 Å
Skewness Skewness skewness0.297
Kurtosis Kurtosis kurtosis-0.506
Angular range angular_range— – 0.3750 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3538000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.933; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.998; Smooth: 0.963
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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8. Citations (1)

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9. Files and Curves (10)