1e7q

GDP 4-keto-6-deoxy-D-mannose epimerase reductase S107A

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

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 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

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.

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 1e7q

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1e7q
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1e7q
Deposition date deposition_date2000-09-07
Structure title titleGDP 4-keto-6-deoxy-D-mannose epimerase reductase S107A
Keywords keywordsEPIMERASE/REDUCTASE, SDR, RED, EPIMERASE-REDUCTASE complex; EPIMERASE/REDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier20.93
Radius of gyration Rg (electron density) rg_electron19.82
Forward intensity I(0) i024956000.00
Molecular weight molecular_weight36616.0 kDa
Excluded volume excluded_volume45121 ų
Envelope volume envelope_volume51990 ų
Hydration-shell volume shell_volume21867 ų
Envelope diameter envelope_diameter70.0
Shell Rg shell_rg26.50
Envelope Rg envelope_rg20.03
Shape Rg shape_rg19.82
Total Rg total_rg20.65
Total atoms total_atoms2566
Residues n_residues314
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_real20.87
Rg uncertainty (real space) rg_real_error0.47
I(0) (real space) i0_real2.4960e+07
I(0) uncertainty (real space) i0_real_error3.0120e+05
Rg (reciprocal space) rg_reciprocal20.89
I(0) (reciprocal space) i0_reciprocal24960000.0000
Solution quality estimate total_estimate0.6318
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.5
Skewness Skewness skewness0.340
Kurtosis Kurtosis kurtosis-0.151
Angular range angular_range— – 0.3800 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha4883000.0000
Real-space data points n_real_points70
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.769; Stabil: 1.000; Sysdev: 0.301; Positv: 1.000; Valcen: 1.000; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 3 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1e7qa_
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_id1e7qA01
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_id1e7qA02
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

8. Citations (1)

9. Files and Curves (10)