8yki

FGFR-1 in complex with ligand tasurgratinib

Method: X-RAY DIFFRACTION Dmax: 91.7 Å Quality: EXCELLENT

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

Fibroblast growth factor receptor 1

Homo sapiens

UniProt P11362

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 461–774 Mutation:C488A A1LY1 Tasurgratinib × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;18% w/v PEG 3350, 0.2M (NH4)2 TARTRATE Resolution 2.79 Å R-free 0.288
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 461–774 Mutation:C488A A1LY1 Tasurgratinib × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;293 K;18% w/v PEG 3350, 0.2M (NH4)2 TARTRATE Resolution 2.79 Å R-free 0.288

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.

77 other PDB entries and 149 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FGFR1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 4–317; UniProt 461–774 Author chain B; PDBConstruct 4–317; UniProt 461–774

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 8yki

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id8yki
Deposition date deposition_date2024-03-05
最后修订 last_revision2024-06-12
Structure title titleFGFR-1 in complex with ligand tasurgratinib
Keywords keywordsFGF RECEPTOR KINASE, PROTEROS BIOSTRUCTURES GMBH, TRANSFERASE; TRANSFERASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier29.58
Radius of gyration Rg (electron density) rg_electron28.84
Forward intensity I(0) i060187000.00
Molecular weight molecular_weight61626.0 kDa
Excluded volume excluded_volume77726 ų
Envelope volume envelope_volume102970 ų
Hydration-shell volume shell_volume30054 ų
Envelope diameter envelope_diameter94.8
Shell Rg shell_rg35.68
Envelope Rg envelope_rg28.48
Shape Rg shape_rg28.83
Total Rg total_rg29.59
Total atoms total_atoms4320
Residues n_residues533
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 dmax91.7
Rg (real space) rg_real29.56
Rg uncertainty (real space) rg_real_error0.80
I(0) (real space) i0_real6.0190e+07
I(0) uncertainty (real space) i0_real_error9.8150e+05
Rg (reciprocal space) rg_reciprocal29.57
I(0) (reciprocal space) i0_reciprocal60190000.0000
Solution quality estimate total_estimate0.9082
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary27.2
Skewness Skewness skewness0.215
Kurtosis Kurtosis kurtosis-0.672
Angular range angular_range— – 0.2700 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha32680000.0000
Real-space data points n_real_points55
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.961; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.984; Smooth: 0.936

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

8. Citations (1)

9. Files and Curves (10)