3bag

Crystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor

Method: X-RAY DIFFRACTION Dmax: 70.4 Å Quality: GOOD

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

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 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain A; UniProt 16–155 Mutation:K112N, N114A FMT FORMIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298.15 K;3.8M Na-formate, 0.2M (NH4)2SO4, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.15K Resolution 1.75 Å R-free 0.224
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 16–155 Mutation:K112N, N114A FMT FORMIC ACID × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;298.15 K;3.8M Na-formate, 0.2M (NH4)2SO4, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.15K Resolution 1.75 Å R-free 0.224

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 216 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FGF1_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 7–146; UniProt 16–155 Author chain B; PDBConstruct 7–146; UniProt 16–155

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 3bag

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3bag
Deposition date deposition_date2007-11-07
Structure title titleCrystal structure of K112N/N114A mutant of Human acidic fibroblast growth factor
Keywords keywords;beta-trefoil, Acetylation, Angiogenesis, Developmental protein, Differentiation, Growth factor, Heparin-binding, Mitogen, Polymorphism, HORMONE ;; HORMONE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.31
Radius of gyration Rg (electron density) rg_electron20.87
Forward intensity I(0) i018519400.00
Molecular weight molecular_weight32228.0 kDa
Excluded volume excluded_volume40086 ų
Envelope volume envelope_volume46613 ų
Hydration-shell volume shell_volume19161 ų
Envelope diameter envelope_diameter71.1
Shell Rg shell_rg26.54
Envelope Rg envelope_rg21.03
Shape Rg shape_rg20.87
Total Rg total_rg21.58
Total atoms total_atoms2276
Residues n_residues274
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 dmax70.4
Rg (real space) rg_real21.33
Rg uncertainty (real space) rg_real_error0.55
I(0) (real space) i0_real1.8520e+07
I(0) uncertainty (real space) i0_real_error2.4510e+05
Rg (reciprocal space) rg_reciprocal21.33
I(0) (reciprocal space) i0_reciprocal18520000.0000
Solution quality estimate total_estimate0.8741
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.8
Skewness Skewness skewness0.367
Kurtosis Kurtosis kurtosis-0.446
Angular range angular_range— – 0.3750 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha5822000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.803; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.971; Smooth: 0.985

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (4 domains)

Domain ID domain_idd3baga1
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_idd3baga2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags
Domain ID domain_idd3bagb1
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_idd3bagb2
Class classl — Artifacts
Fold Fold foldl.1 — Tags
Superfamily Superfamily superfamilyl.1.1 — Tags
Family Family familyl.1.1.1 — Tags

CATH v4.4 (2 domains)

Domain ID domain_id3bagA00
Class class2 — Mainly Beta
Architecture architecture80 — Trefoil
Topology topology10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily50
Domain ID domain_id3bagB00
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)