9eko

A chimeric hybrid protein fused with the FGFR3 Transmembrane Domain

Method: X-RAY DIFFRACTION Dmax: 89.5 Å Quality: GOOD

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

chimeric protein fused with the FGFR3 Transmembrane Domain,Saposin-A,Fibroblast growth factor receptor 3

Homo sapiens

UniProt P07602

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 79–139 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.90 Å R-free 0.287

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.

20 other PDB entries and 31 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SAP_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 381–441; UniProt 79–139

chimeric protein fused with the FGFR3 Transmembrane Domain,Saposin-A,Fibroblast growth factor receptor 3

Homo sapiens

UniProt P0AEX9

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 27–387 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.90 Å R-free 0.287

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.

366 other PDB entries and 491 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name MALE_ECOLI
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 3–363; UniProt 27–387

chimeric protein fused with the FGFR3 Transmembrane Domain,Saposin-A,Fibroblast growth factor receptor 3

Homo sapiens

UniProt P22607

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Insufficient information Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain A; UniProt 371–399 Not recorded alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 2.90 Å R-free 0.287

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 28 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FGFR3_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 447–475; UniProt 371–399

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 9eko

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9eko
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id9eko
Deposition date deposition_date2024-12-03
最后修订 last_revision2026-06-10
Structure title titleA chimeric hybrid protein fused with the FGFR3 Transmembrane Domain
Keywords keywordschimeric hybrid protein, Fibroblast growth factor receptor, MEMBRANE PROTEIN; MEMBRANE PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.05
Radius of gyration Rg (electron density) rg_electron24.17
Forward intensity I(0) i036829300.00
Molecular weight molecular_weight47778.0 kDa
Excluded volume excluded_volume60139 ų
Envelope volume envelope_volume72799 ų
Hydration-shell volume shell_volume25901 ų
Envelope diameter envelope_diameter93.7
Shell Rg shell_rg30.16
Envelope Rg envelope_rg24.97
Shape Rg shape_rg24.15
Total Rg total_rg24.95
Total atoms total_atoms6593
Residues n_residues452
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 dmax89.5
Rg (real space) rg_real25.12
Rg uncertainty (real space) rg_real_error0.75
I(0) (real space) i0_real3.6830e+07
I(0) uncertainty (real space) i0_real_error5.5370e+05
Rg (reciprocal space) rg_reciprocal25.10
I(0) (reciprocal space) i0_reciprocal36830000.0000
Solution quality estimate total_estimate0.8417
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary27.0
Skewness Skewness skewness0.521
Kurtosis Kurtosis kurtosis0.114
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5840000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.690; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.885; Smooth: 0.983

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)