1bfc

BASIC FIBROBLAST GROWTH FACTOR COMPLEXED WITH HEPARIN HEXAMER FRAGMENT

Method: X-RAY DIFFRACTION D_max: 48.9 Å Quality: GOOD

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

BASIC FIBROBLAST GROWTH FACTOR

OrganismNot specified

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 9–155	Mutation：C70S, C88S	;4-deoxy-2-O-sulfo-alpha-L-threo-hex-4-enopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose ; × 1	X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions	Resolution 2.20 Å

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.

Other PDB	Difference from Current Entry 1BFC	Assembly / Oligomeric State	Construct	Mutations and Modifications	Ligands, Ions and Non-polymers	Method and Experimental Conditions	Structure Quality
1BAS THREE-DIMENSIONAL STRUCTURES OF ACIDIC AND BASIC FIBROBLAST GROWTH FACTORS Deposited 1992-09-29	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 2–155（154 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.90 Å
1BFB BASIC FIBROBLAST GROWTH FACTOR COMPLEXED WITH HEPARIN TETRAMER FRAGMENT Deposited 1995-12-12	Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 9–155（147 aa）	Mutation：C70S, C88S	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.90 Å
1BFF THE 154 AMINO ACID FORM OF HUMAN BASIC FIBROBLAST GROWTH FACTOR Deposited 1996-12-06	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 27–155（129 aa）	Not recorded	PO4 PHOSPHATE ION × 1 BME BETA-MERCAPTOETHANOL × 1	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；THE PROTEIN WAS CRYSTALLIZED FROM 30-40 % PEG1000 AND 0.2-0.3 % 2-MERCAPTOETHANOL BY THE HANGING DROP VAPOR DIFFUSION METHOD., pH 7.5, vapor diffusion - hanging drop	Resolution 2.00 Å
1BFG CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION Deposited 1993-04-15	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 10–155（146 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.60 Å
1BLA BASIC FIBROBLAST GROWTH FACTOR (FGF-2) MUTANT WITH CYS 78 REPLACED BY SER AND CYS 96 REPLACED BY SER, NMR Deposited 1996-05-20	Different construct Different mutation/modification Different oligomeric state Different experimental method Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–155（155 aa）	Mutation：C78S, C96S	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1BLD BASIC FIBROBLAST GROWTH FACTOR (FGF-2) MUTANT WITH CYS 78 REPLACED BY SER AND CYS 96 REPLACED BY SER, NMR Deposited 1996-05-20	Different construct Different mutation/modification Different oligomeric state Different experimental method Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 1–155（155 aa）	Mutation：C78S, C96S	No recorded non-water small molecule	SOLUTION NMR mmCIF provides none of the parsed conditions	Resolution not provided
1CVS CRYSTAL STRUCTURE OF A DIMERIC FGF2-FGFR1 COMPLEX Deposited 1999-08-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 24–155（132 aa） Chain B 24–155（132 aa）	Mutation：YES Mutation：YES	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；ammonium sulfate, glycerol, Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.80 Å R-free 0.281
1CVS CRYSTAL STRUCTURE OF A DIMERIC FGF2-FGFR1 COMPLEX Deposited 1999-08-24	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 24–155（132 aa） Chain B 24–155（132 aa）	Mutation：YES Mutation：YES	SO4 SULFATE ION × 8	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；ammonium sulfate, glycerol, Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K	Resolution 2.80 Å R-free 0.281
1EV2 CRYSTAL STRUCTURE OF FGF2 IN COMPLEX WITH THE EXTRACELLULAR LIGAND BINDING DOMAIN OF FGF RECEPTOR 2 (FGFR2) Deposited 2000-04-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 8 PDB declaration: octameric	Chain A 24–155（132 aa） Fragment：THE B-TREFOIL CORE OF FIBROBLAST GROWTH FACTOR 2 Chain B 24–155（132 aa） Fragment：THE B-TREFOIL CORE OF FIBROBLAST GROWTH FACTOR 2 Chain C 24–155（132 aa） Fragment：THE B-TREFOIL CORE OF FIBROBLAST GROWTH FACTOR 2 Chain D 24–155（132 aa） Fragment：THE B-TREFOIL CORE OF FIBROBLAST GROWTH FACTOR 2	Mutation：YES Mutation：YES Mutation：YES Mutation：YES	SO4 SULFATE ION × 4	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, temperature 298.0K	Resolution 2.20 Å R-free 0.273
1FGA REFINEMENT OF THE STRUCTURE OF HUMAN BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION AND ANALYSIS OF PRESUMED HEPARIN BINDING SITES BY SELENATE SUBSTITUTION Deposited 1993-02-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 10–155（146 aa）	Not recorded	SE4 SELENATE ION × 2 BME BETA-MERCAPTOETHANOL × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.20 Å
1FQ9 CRYSTAL STRUCTURE OF A TERNARY FGF2-FGFR1-HEPARIN COMPLEX Deposited 2000-09-04	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 24–155（132 aa） Fragment：THE B-TREFOIL CORE OF FIBROBLAST GROWTH FACTOR 2 (FGF2) Chain B 24–155（132 aa） Fragment：THE B-TREFOIL CORE OF FIBROBLAST GROWTH FACTOR 2 (FGF2)	Mutation：C69S, C87S Mutation：C69S, C87S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 8.5；298 K；Ammonium sulfate, Glycerol, Tris-HCl, pH 8.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 3.00 Å R-free 0.282
1II4 CRYSTAL STRUCTURE OF SER252TRP APERT MUTANT FGF RECEPTOR 2 (FGFR2) IN COMPLEX WITH FGF2 Deposited 2001-04-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–155（155 aa）	Mutation：C78S,C96S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.70 Å R-free 0.267
1II4 CRYSTAL STRUCTURE OF SER252TRP APERT MUTANT FGF RECEPTOR 2 (FGFR2) IN COMPLEX WITH FGF2 Deposited 2001-04-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–155（155 aa）	Mutation：C78S,C96S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.70 Å R-free 0.267
1II4 CRYSTAL STRUCTURE OF SER252TRP APERT MUTANT FGF RECEPTOR 2 (FGFR2) IN COMPLEX WITH FGF2 Deposited 2001-04-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–155（155 aa）	Mutation：C78S,C96S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.70 Å R-free 0.267
1II4 CRYSTAL STRUCTURE OF SER252TRP APERT MUTANT FGF RECEPTOR 2 (FGFR2) IN COMPLEX WITH FGF2 Deposited 2001-04-20	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–155（155 aa）	Mutation：C78S,C96S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.70 Å R-free 0.267
1IIL CRYSTAL STRUCTURE OF PRO253ARG APERT MUTANT FGF RECEPTOR 2 (FGFR2) IN COMPLEX WITH FGF2 Deposited 2001-04-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain A 1–155（155 aa）	Mutation：C78S,C96S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.30 Å R-free 0.259
1IIL CRYSTAL STRUCTURE OF PRO253ARG APERT MUTANT FGF RECEPTOR 2 (FGFR2) IN COMPLEX WITH FGF2 Deposited 2001-04-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 2 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 1–155（155 aa）	Mutation：C78S,C96S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.30 Å R-free 0.259
1IIL CRYSTAL STRUCTURE OF PRO253ARG APERT MUTANT FGF RECEPTOR 2 (FGFR2) IN COMPLEX WITH FGF2 Deposited 2001-04-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 3 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain C 1–155（155 aa）	Mutation：C78S,C96S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.30 Å R-free 0.259
1IIL CRYSTAL STRUCTURE OF PRO253ARG APERT MUTANT FGF RECEPTOR 2 (FGFR2) IN COMPLEX WITH FGF2 Deposited 2001-04-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 4 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain D 1–155（155 aa）	Mutation：C78S,C96S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 7.5；298 K；PEG 4000, Isopropanol, HEPES-NaOH, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298.0K	Resolution 2.30 Å R-free 0.259
2BFH CRYSTAL STRUCTURE OF BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION Deposited 1993-08-31	Different construct Different mutation/modification Different oligomeric state Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 28–155（128 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 2.50 Å
2FGF THREE-DIMENSIONAL STRUCTURE OF HUMAN BASIC FIBROBLAST GROWTH FACTOR, A STRUCTURAL HOMOLOG OF INTERLEUKIN 1BETA Deposited 1991-02-19	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 10–155（146 aa）	Not recorded	SO4 SULFATE ION × 3	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.77 Å
2M49 Structural Insights into Human S100B and Basic Fibroblast Growth Factor (FGF2) Interaction Deposited 2013-02-03	Different construct Different mutation/modification Different oligomeric state Different experimental method Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 4 PDB declaration: tetrameric	Chain A 161–286（126 aa） Fragment：UNP residues 161-286 Chain C 161–286（126 aa） Fragment：UNP residues 161-286	Mutation：C211S, C229S Mutation：C211S, C229S	No recorded non-water small molecule	SOLUTION NMR NMR measurement conditions pH 7.2；298 K；Ionic strength (raw mmCIF value) 0.050；Pressure ambient NMR sample composition 1.2 mM [U-100% 13C; U-100% 15N] S100B-1, 20 mM TRIS-2, 50 mM ammonium sulfate-3, 5 mM calcium chloride-4, 5 mM DTT-5, 0.01 % sodium azide-6, 90% H2O/10% D2O \| 90% H2O/10% D2O	Resolution not provided
4FGF REFINEMENT OF THE STRUCTURE OF HUMAN BASIC FIBROBLAST GROWTH FACTOR AT 1.6 ANGSTROMS RESOLUTION AND ANALYSIS OF PRESUMED HEPARIN BINDING SITES BY SELENATE SUBSTITUTION Deposited 1993-02-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 10–155（146 aa）	Not recorded	SO4 SULFATE ION × 1 BME BETA-MERCAPTOETHANOL × 2	X-RAY DIFFRACTION mmCIF provides none of the parsed conditions	Resolution 1.60 Å
4OEE Crystal Structure Analysis of FGF2-Disaccharide (S3I2) complex Deposited 2014-01-13	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 134–288（155 aa） Fragment：unp residues 134-288	Mutation：C69S, C87S	No recorded non-water small molecule	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 1.50 Å R-free 0.185
4OEF Crystal Structure Analysis of FGF2-Disaccharide (S6I2) complex Deposited 2014-01-13	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 134–288（155 aa）	Mutation：C69S, C87S	No recorded non-water small molecule	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
4OEG Crystal Structure Analysis of FGF2-Disaccharide (S9I2) complex Deposited 2014-01-13	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 1 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain A 134–288（155 aa） Fragment：unp residues 134-288	Mutation：C69S, C87S	No recorded non-water small molecule	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 1.60 Å R-free 0.215
5X1O PI(4,5)P2 lipid binding induced a reorientation of FGF2 molecules near membrane surface to facilitate the unconventional oligomerization-dependent secretion process as revealed by a combined FTIR/NMR/X-ray study Deposited 2017-01-26	Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics	Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric	Chain A 143–288（146 aa） Chain B 143–288（146 aa）	Not recorded	I3P D-MYO-INOSITOL-1,4,5-TRIPHOSPHATE × 2	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；298 K；0.1M Sodium citrate, 0.2M Ammonium acetate, 30% PEG 4000	Resolution 1.90 Å R-free 0.276
6L4O Crystal structure of API5-FGF2 complex Deposited 2019-10-18	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein heterocomplex Heteromer；Protein × 2 PDB declaration: dimeric	Chain B 135–288（154 aa）	Mutation：C211S,C229S	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；277 K；100mM Na-HEPES (pH 7.5), 100mM potassium chloride, 10% (v/v) polyethylene glycol (PEG) 6000	Resolution 2.60 Å R-free 0.262
8HU7 Crystal structure of FGF2-M1 mutant - D28E/C78L/C96I/S137P Deposited 2022-12-22	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 143–288（146 aa）	Mutation：D28E/C78I/C96I/S137P	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；pH 5.5；289.15 K；1.5M sodium citrate, 100mM sodium cacodylate, pH 5.5	Resolution 1.40 Å R-free 0.213
8HUE Crystal structure of FGF2-M2 mutant - D28E/C78I/C96I/S137P Deposited 2022-12-23	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 143–288（146 aa）	Mutation：D28E/C78I/C96I/S137P	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；289.15 K；30% (w/v) polyethylene glycol 2000, 100mM potassium thiocyanate	Resolution 1.48 Å R-free 0.196
8HUE Crystal structure of FGF2-M2 mutant - D28E/C78I/C96I/S137P Deposited 2022-12-23	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 2 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain B 143–288（146 aa）	Mutation：D28E/C78I/C96I/S137P	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；289.15 K；30% (w/v) polyethylene glycol 2000, 100mM potassium thiocyanate	Resolution 1.48 Å R-free 0.196
8HUE Crystal structure of FGF2-M2 mutant - D28E/C78I/C96I/S137P Deposited 2022-12-23	Different construct Different mutation/modification Different experimental conditions Different structure-quality metrics	Assembly 3 Other combination Monomer；Protein × 1 PDB declaration: monomeric	Chain C 143–288（146 aa）	Mutation：D28E/C78I/C96I/S137P	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions MICROBATCH；289.15 K；30% (w/v) polyethylene glycol 2000, 100mM potassium thiocyanate	Resolution 1.48 Å R-free 0.196
8OM6 Crystal structure of FGF2-STAB, a stable variant of human fibroblast growth factor 2 Deposited 2023-03-31	Different construct Different mutation/modification Different oligomeric state Different experimental conditions Different structure-quality metrics	Assembly 1 Protein monomer Monomer；Protein × 1 PDB declaration: monomeric	Chain A 134–288（155 aa）	Not recorded	No recorded non-water small molecule	X-RAY DIFFRACTION X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；pH 6.3；292.15 K；PEG 3350, Bis-Tris	Resolution 1.31 Å R-free 0.227

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 1–147； UniProt 9–155

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

P(r) Distance Distribution P(r) Distribution

Download Download SAXS (.dat) P(r) (.pr.out) CIF

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2. Structure Basics 2. Structure Basics

Entry ID entry_id	1bfc
Deposition date deposition_date	1995-12-12
Structure title title	BASIC FIBROBLAST GROWTH FACTOR COMPLEXED WITH HEPARIN HEXAMER FRAGMENT
Keywords keywords	GROWTH FACTOR, MITOGEN, VASCULARIZATION, HEPARIN-BINDING; GROWTH FACTOR
Experimental Method method	X-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier	15.64 Å
Radius of gyration Rg (electron density) rg_electron	14.02 Å
Forward intensity I(0) i0	5566990.00
Molecular weight molecular_weight	15856.0 kDa
Excluded volume excluded_volume	19356 Å³
Envelope volume envelope_volume	21308 Å³
Hydration-shell volume shell_volume	12849 Å³
Envelope diameter envelope_diameter	48.0 Å
Shell Rg shell_rg	19.94 Å
Envelope Rg envelope_rg	14.27 Å
Shape Rg shape_rg	13.90 Å
Total Rg total_rg	15.41 Å
Total atoms total_atoms	1100
Residues n_residues	124
Spherical-harmonic order n_harmonics	20
q range q_range	— – 0.5000 Å⁻¹
Data points n_points	101
Shell type shell_type	directional
Solvent electron density solvent_density	0.3340 e/Å³
Shell contrast contrast_shell	0.0300 e/Å³
CRYSOL version crysol_version	4.1.3

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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax	48.9 Å
Rg (real space) rg_real	15.53 Å
Rg uncertainty (real space) rg_real_error	0.21 Å
I(0) (real space) i0_real	5.5670e+06
I(0) uncertainty (real space) i0_real_error	5.6010e+04
Rg (reciprocal space) rg_reciprocal	15.55 Å
I(0) (reciprocal space) i0_reciprocal	5567000.0000
Solution quality estimate total_estimate	0.8960
Solution quality rating solution_quality	GOOD a GOOD solution
P(r) peaks n_peaks	2
Primary peak position r_peak_primary	21.0 Å
Skewness Skewness skewness	0.100
Kurtosis Kurtosis kurtosis	-0.411
Angular range angular_range	— – 0.5000 Å⁻¹
Current regularization parameter α current_alpha	0.0000
Highest regularization parameter α highest_alpha	915300.0000
Real-space data points n_real_points	80
GNOM version gnom_version	4.1.3
Quality Criteria quality_criteria	AN1: 0.000; Oscil: 0.891; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.994; Smooth: 0.978

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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

Entity 1 Entity 1 polymer

Description description	BASIC FIBROBLAST GROWTH FACTOR
Molecular weight formula_weight	16516.9 kDa
Mutation mutation	C70S, C88S
Source method src_method	nat
Copy count entity_count	1

Polymer Polymer

Polymer type type	polypeptide(L)
Chain IDs strand_id	A
Atom count atom_count	1114

LPALPEDGGSGAFPPGHFKDPKRLYCKNGGFFLRIHPDGRVDGVREKSDPHIKLQLQAEERGVVSIKGVSANRYLAMKEDGRLLASKSVTDECFFFERLESNNYNTYRSRKYTSWYVALKRTGQYKLGSKTGPGQKAILFLPMSAKS

Entity 2 Entity 2 branched

Description description	;4-deoxy-2-O-sulfo-alpha-L-threo-hex-4-enopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose-(1-4)-2-O-sulfo-alpha-L-idopyranuronic acid-(1-4)-2-deoxy-6-O-sulfo-2-(sulfoamino)-alpha-D-glucopyranose ;
Molecular weight formula_weight	1732.4 kDa
Source method src_method	man
Copy count entity_count	1

Entity 3 Entity 3 water

Description description	water
Molecular weight formula_weight	18.0 kDa
Source method src_method	nat
Copy count entity_count	14

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7. Fold Classification (SCOP + CATH) 2 domains

SCOP 2.08 (1 domains)

Domain ID domain_id	d1bfca_
Class class	b — All beta proteins
Fold Fold fold	b.42 — beta-Trefoil
Superfamily Superfamily superfamily	b.42.1 — Cytokine
Family Family family	b.42.1.1 — Fibroblast growth factors (FGF)

CATH v4.4 (1 domains)

Domain ID domain_id	1bfcA00
Class class	2 — Mainly Beta
Architecture architecture	80 — Trefoil
Topology topology	10 — Trefoil (Acidic Fibroblast Growth Factor, subunit A)
Homologous superfamily homologous superfamily	50 —

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8. Citations (2)

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Unit-cell length a length_a	33.150 Å
Unit-cell length b length_b	41.800 Å
Unit-cell length c length_c	85.900 Å
Unit-cell angle α angle_alpha	90.00 °
Unit-cell angle β angle_beta	90.00 °
Unit-cell angle γ angle_gamma	90.00 °
Molecules per unit cell Z z_pdb	4

Space group space_group	P 21 21 21
Space-group number int_tables_number	19
Crystal system crystal_system	—

Resolution resolution	2.200 Å
Low-resolution limit resolution_low	6.000 Å
R factor r_factor	0.1880
R_work r_work	0.1880
R_free r_free	—

fit	/app/data/saxs_computation/bf/1bfc/1bfc.fit
pddf	/app/data/pr_computation/bf/1bfc/1bfc.pr.out
profile	/app/data/saxs_computation/bf/1bfc/1bfc.dat