4oef

Crystal Structure Analysis of FGF2-Disaccharide (S6I2) complex

Method: X-RAY DIFFRACTION Dmax: 45.1 Å Quality: GOOD

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

Fibroblast growth factor 2

Homo sapiens

UniProt P09038

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 Monomer Protein × 1 其他Polymer 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 134–288 Mutation:C69S, C87S 2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-1-O-methyl-2-O-sulfo-alpha-L-idopyranuronic acid × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 4.2;299 K;40% polyethylene glycol 600 and 100 mM Na2HPO4/citric acid, pH 4.2, VAPOR DIFFUSION, HANGING DROP, temperature 299K Resolution 1.80 Å R-free 0.220

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.

24 other PDB entries and 33 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FGF2_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–155; UniProt 134–288

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 4oef

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4oef
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4oef
Deposition date deposition_date2014-01-13
Structure title titleCrystal Structure Analysis of FGF2-Disaccharide (S6I2) complex
Keywords keywordsHeparin/Heparin Sulfate Binding, 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_guinier15.04
Radius of gyration Rg (electron density) rg_electron13.48
Forward intensity I(0) i04657030.00
Molecular weight molecular_weight14930.0 kDa
Excluded volume excluded_volume18539 ų
Envelope volume envelope_volume20437 ų
Hydration-shell volume shell_volume12611 ų
Envelope diameter envelope_diameter43.6
Shell Rg shell_rg19.59
Envelope Rg envelope_rg13.80
Shape Rg shape_rg13.42
Total Rg total_rg14.87
Total atoms total_atoms1046
Residues n_residues125
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 dmax45.1
Rg (real space) rg_real14.90
Rg uncertainty (real space) rg_real_error0.18
I(0) (real space) i0_real4.6570e+06
I(0) uncertainty (real space) i0_real_error4.7180e+04
Rg (reciprocal space) rg_reciprocal14.91
I(0) (reciprocal space) i0_reciprocal4657000.0000
Solution quality estimate total_estimate0.8944
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.1
Skewness Skewness skewness0.020
Kurtosis Kurtosis kurtosis-0.429
Angular range angular_range— – 0.5000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha1160000.0000
Real-space data points n_real_points80
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.903; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.936

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd4oefa_
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 (1 domains)

Domain ID domain_id4oefA00
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)