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1gfs

GDP-FUCOSE SYNTHETASE FROM E. COLI

Method: X-RAY DIFFRACTION Dmax: 67.9 Å Quality: REASONABLE
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1. Protein Identity and Related Structures Protein Identity & Related Structures

GDP-FUCOSE SYNTHETASE

Escherichia coli

UniProt P32055

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 homooligomer Homooligomer Protein × 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 1–321 Not recorded No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions：pH 7；pH 7.00 Resolution 2.20 Å R-free 0.214

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 1GFS Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
1BSV GDP-FUCOSE SYNTHETASE FROM ESCHERICHIA COLI COMPLEX WITH NADPH Deposited 1998-08-31 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–321（321 aa）
Not recorded NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；4.0 M SODIUM FORMATE, pH 7
Resolution 2.20 Å
1BWS CRYSTAL STRUCTURE OF GDP-4-KETO-6-DEOXY-D-MANNOSE EPIMERASE/REDUCTASE FROM ESCHERICHIA COLI A KEY ENZYME IN THE BIOSYNTHESIS OF GDP-L-FUCOSE Deposited 1998-09-25 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–321（321 aa）
Not recorded NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.5
Resolution 2.20 Å
1BWS CRYSTAL STRUCTURE OF GDP-4-KETO-6-DEOXY-D-MANNOSE EPIMERASE/REDUCTASE FROM ESCHERICHIA COLI A KEY ENZYME IN THE BIOSYNTHESIS OF GDP-L-FUCOSE Deposited 1998-09-25 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–321（321 aa）
Not recorded NDP NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；pH 6.5
Resolution 2.20 Å
1E6U GDP 4-keto-6-deoxy-D-mannose epimerase reductase Deposited 2000-08-23 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–321（321 aa）
Not recorded NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 UVW ACETYLPHOSPHATE × 2 SO4 SULFATE ION × 8 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；294 K；1.5 M LITHIUM SULPHATE, PH 6.5 0.1M TRIS BUFFER 21C
Resolution 1.45 Å R-free 0.170
1E7Q GDP 4-keto-6-deoxy-D-mannose epimerase reductase S107A Deposited 2000-09-07 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–321（321 aa）
Mutation：YES NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 UVW ACETYLPHOSPHATE × 2 SO4 SULFATE ION × 8 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；294 K；1.5 M LITHIUM SULPHATE, PH 6.5 0.1M TRIS BUFFER, 21C
Resolution 1.60 Å R-free 0.182
1E7R GDP 4-keto-6-deoxy-D-mannose epimerase reductase Y136E Deposited 2000-09-07 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–321（321 aa）
Mutation：YES NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 UVW ACETYLPHOSPHATE × 2 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 4 SO4 SULFATE ION × 4 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；294 K；1.5 M LITHIUM SULPHATE, PH 6.5 0.1M TRIS BUFFER 21C
Resolution 1.60 Å R-free 0.180
1E7S GDP 4-keto-6-deoxy-D-mannose epimerase reductase K140R Deposited 2000-09-07 Different mutation/modification Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–321（321 aa）
Mutation：YES NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 UVW ACETYLPHOSPHATE × 2 SO4 SULFATE ION × 6 TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 6.5；294 K；1.5 M LITHIUM SULPHATE, PH 6.5 0.1M TRIS BUFFER 21C
Resolution 1.50 Å R-free 0.162
1FXS GDP-FUCOSE SYNTHETASE FROM ESCHERICHIA COLI COMPLEX WITH NADP Deposited 1998-09-01 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–321（321 aa）
Not recorded NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；4.0 M SODIUM FORMATE, pH 7
Resolution 2.30 Å
1FXS GDP-FUCOSE SYNTHETASE FROM ESCHERICHIA COLI COMPLEX WITH NADP Deposited 1998-09-01 Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 2 Protein homooligomer Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–321（321 aa）
Not recorded NAP NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE × 2 X-RAY DIFFRACTION
X-ray crystallization conditions pH 7；4.0 M SODIUM FORMATE, pH 7
Resolution 2.30 Å

7 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name FCL_ECOLI
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–321； UniProt 1–321

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 1gfs

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1gfs
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1gfs
Deposition date deposition_date1998-08-17
Structure title titleGDP-FUCOSE SYNTHETASE FROM E. COLI
Keywords keywordsEPIMERASE-REDUCTASE, NADP, GDP-FUCOSE, LIPOPOLYSACCHARIDE BIOSYNTHESIS, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier21.07 Å
Radius of gyration Rg (electron density) rg_electron19.92 Å
Forward intensity I(0) i021871300.00
Molecular weight molecular_weight35315.0 kDa
Excluded volume excluded_volume44075 ų
Envelope volume envelope_volume51816 ų
Hydration-shell volume shell_volume21779 ų
Envelope diameter envelope_diameter68.1 Å
Shell Rg shell_rg26.49 Å
Envelope Rg envelope_rg19.97 Å
Shape Rg shape_rg19.94 Å
Total Rg total_rg20.75 Å
Total atoms total_atoms2489
Residues n_residues317
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax67.9 Å
Rg (real space) rg_real21.00 Å
Rg uncertainty (real space) rg_real_error0.31 Å
I(0) (real space) i0_real2.1870e+07
I(0) uncertainty (real space) i0_real_error2.9050e+05
Rg (reciprocal space) rg_reciprocal21.01 Å
I(0) (reciprocal space) i0_reciprocal21870000.0000
Solution quality estimate total_estimate0.7106
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.9 Å
Skewness Skewness skewness0.291
Kurtosis Kurtosis kurtosis-0.243
Angular range angular_range— – 0.3750 Å−1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha3973000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.855; Stabil: 1.000; Sysdev: 0.225; Positv: 1.000; Valcen: 1.000; Smooth: 0.996
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (2)

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7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1gfsa_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.2 — NAD(P)-binding Rossmann-fold domains
Superfamily Superfamily superfamilyc.2.1 — NAD(P)-binding Rossmann-fold domains
Family Family familyc.2.1.2 — Tyrosine-dependent oxidoreductases

CATH v4.4 (2 domains)

Domain ID domain_id1gfsA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily720 — NAD(P)-binding Rossmann-like Domain
Domain ID domain_id1gfsA02
Class class3 — Alpha Beta
Architecture architecture90 — Alpha-Beta Complex
Topology topology25 — UDP-galactose 4-epimerase; domain 1
Homologous superfamily homologous superfamily10 — UDP-galactose 4-epimerase, domain 1
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8. Citations (1)

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9. Files and Curves (10)