1bgt

CRYSTAL STRUCTURE OF THE DNA MODIFYING ENZYME BETA-GLUCOSYLTRANSFERASE IN THE PRESENCE AND ABSENCE OF THE SUBSTRATE URIDINE DIPHOSPHOGLUCOSE

Method: X-RAY DIFFRACTION Dmax: 67.9 Å Quality: REASONABLE

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

BETA-GLUCOSYLTRANSFERASE

Enterobacteria phage T4

UniProt P04547

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 1–351 Not recorded No other associated polymer 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.

19 other PDB entries and 22 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name GSTB_BPT4
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–351; UniProt 1–351

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 1bgt

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1bgt
Deposition date deposition_date1994-06-09
Structure title titleCRYSTAL STRUCTURE OF THE DNA MODIFYING ENZYME BETA-GLUCOSYLTRANSFERASE IN THE PRESENCE AND ABSENCE OF THE SUBSTRATE URIDINE DIPHOSPHOGLUCOSE
Keywords keywordsTRANSFERASE(GLYCOSYLTRANSFERASE); TRANSFERASE(GLYCOSYLTRANSFERASE)
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier21.53
Radius of gyration Rg (electron density) rg_electron20.96
Forward intensity I(0) i021716500.00
Molecular weight molecular_weight38067.0 kDa
Excluded volume excluded_volume46947 ų
Envelope volume envelope_volume33532 ų
Hydration-shell volume shell_volume14956 ų
Envelope diameter envelope_diameter67.7
Shell Rg shell_rg24.56
Envelope Rg envelope_rg19.43
Shape Rg shape_rg20.97
Total Rg total_rg21.32
Total atoms total_atoms
Residues n_residues
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 dmax67.9
Rg (real space) rg_real21.50
Rg uncertainty (real space) rg_real_error0.32
I(0) (real space) i0_real2.1720e+07
I(0) uncertainty (real space) i0_real_error2.7590e+05
Rg (reciprocal space) rg_reciprocal21.51
I(0) (reciprocal space) i0_reciprocal21720000.0000
Solution quality estimate total_estimate0.7335
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary25.0
Skewness Skewness skewness0.301
Kurtosis Kurtosis kurtosis-0.408
Angular range angular_range— – 0.3700 −1
Current regularization parameter α current_alpha0.0001
Highest regularization parameter α highest_alpha3941000.0000
Real-space data points n_real_points69
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.921; Stabil: 1.000; Sysdev: 0.281; Positv: 1.000; Valcen: 0.998; Smooth: 0.925

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (1)

7. Fold Classification (SCOP + CATH) 1 domains

SCOP 2.08 (1 domains)

Domain ID domain_idd1bgta_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.87 — UDP-Glycosyltransferase/glycogen phosphorylase
Superfamily Superfamily superfamilyc.87.1 — UDP-Glycosyltransferase/glycogen phosphorylase
Family Family familyc.87.1.1 — beta-Glucosyltransferase (DNA-modifying)

8. Citations (3)

9. Files and Curves (10)