3cu1

Crystal Structure of 2:2:2 FGFR2D2:FGF1:SOS complex

Method: X-RAY DIFFRACTION Dmax: 78.8 Å Quality: EXCELLENT

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

Fibroblast growth factor receptor 2

Homo sapiens

UniProt P21802

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain A; UniProt 150–249 Chain C; UniProt 150–249 Fragment:Ig-like C2-type 2 domain, UNP residues 150-249 Heparin-binding growth factor 1 × 2 (P05230) 1,3,4,6-tetra-O-sulfo-beta-D-fructofuranose-(2-1)-2,3,4,6-tetra-O-sulfonato-alpha-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;12% PEG3350, 4% Tacsimate, pH 7.0, vapor diffusion, hanging drop, temperature 298.0K Resolution 2.60 Å R-free 0.277

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.

60 other PDB entries and 123 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FGFR2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–100; UniProt 150–249 Author chain C; PDBConstruct 1–100; UniProt 150–249

Heparin-binding growth factor 1

Homo sapiens

UniProt P05230

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Heteromer Protein × 4 其他Polymer 2 PDB declaration: tetrameric(4) Consistent with protein copy count Chain B; UniProt 22–152 Chain D; UniProt 22–152 Fragment:UNP residues 22-152 Fibroblast growth factor receptor 2 × 2 (P21802) 1,3,4,6-tetra-O-sulfo-beta-D-fructofuranose-(2-1)-2,3,4,6-tetra-O-sulfonato-alpha-D-glucopyranose × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;298 K;12% PEG3350, 4% Tacsimate, pH 7.0, vapor diffusion, hanging drop, temperature 298.0K Resolution 2.60 Å R-free 0.277

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.

96 other PDB entries and 217 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FGF1_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain B; PDBConstruct 1–131; UniProt 22–152 Author chain D; PDBConstruct 1–131; UniProt 22–152

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 3cu1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3cu1
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3cu1
Deposition date deposition_date2008-04-15
Structure title titleCrystal Structure of 2:2:2 FGFR2D2:FGF1:SOS complex
Keywords keywords;Fibroblast growth factor 1, Fibroblast growth factor receptor 2, D2 domain, sucrose octa sulfate, Alternative splicing, ATP-binding, Disease mutation, Ectodermal dysplasia, Glycoprotein, Heparin-binding, Immunoglobulin domain, Kinase, Lacrimo-auriculo-dento-digital syndrome, Membrane, Nucleotide-binding, Phosphoprotein, Polymorphism, Secreted, Transferase, Transmembrane, Tyrosine-protein kinase, Acetylation, Angiogenesis, Developmental protein, Differentiation, Mitogen, Transferase-Hormone COMPLEX ;; Transferase/Hormone
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier25.04
Radius of gyration Rg (electron density) rg_electron24.60
Forward intensity I(0) i054834300.00
Molecular weight molecular_weight54528.0 kDa
Excluded volume excluded_volume67045 ų
Envelope volume envelope_volume83969 ų
Hydration-shell volume shell_volume28381 ų
Envelope diameter envelope_diameter81.5
Shell Rg shell_rg31.92
Envelope Rg envelope_rg24.64
Shape Rg shape_rg24.66
Total Rg total_rg25.24
Total atoms total_atoms3811
Residues n_residues459
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 dmax78.8
Rg (real space) rg_real24.96
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real5.4830e+07
I(0) uncertainty (real space) i0_real_error7.9980e+05
Rg (reciprocal space) rg_reciprocal24.99
I(0) (reciprocal space) i0_reciprocal54840000.0000
Solution quality estimate total_estimate0.9022
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary28.8
Skewness Skewness skewness0.221
Kurtosis Kurtosis kurtosis-0.405
Angular range angular_range— – 0.3150 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha8930000.0000
Real-space data points n_real_points64
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.917; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 1.000; Smooth: 0.973

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 8 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd3cu1a_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.4 — I set domains
Domain ID domain_idd3cu1b_
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.1 — Cytokine
Family Family familyb.42.1.1 — Fibroblast growth factors (FGF)
Domain ID domain_idd3cu1c_
Class classb — All beta proteins
Fold Fold foldb.1 — Immunoglobulin-like beta-sandwich
Superfamily Superfamily superfamilyb.1.1 — Immunoglobulin
Family Family familyb.1.1.4 — I set domains
Domain ID domain_idd3cu1d_
Class classb — All beta proteins
Fold Fold foldb.42 — beta-Trefoil
Superfamily Superfamily superfamilyb.42.1 — Cytokine
Family Family familyb.42.1.1 — Fibroblast growth factors (FGF)

CATH v4.4 (4 domains)

Domain ID domain_id3cu1A01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3cu1B00
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50
Domain ID domain_id3cu1C01
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily10 — Immunoglobulins
Domain ID domain_id3cu1D00
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50

8. Citations (1)

9. Files and Curves (10)