1sxp

BGT in complex with a 13mer DNA containing a central A:G mismatch

Method: X-RAY DIFFRACTION Dmax: 98.2 Å Quality: EXCELLENT

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

DNA 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–DNA Homooligomer Protein × 2 DNA 2 PDB declaration: tetrameric(4) Consistent with all polymer counts Chain A; UniProt 1–351 Chain B; UniProt 1–351 Not recorded 5'-D(*A*AP*TP*AP*CP*TP*AP*AP*GP*AP*TP*AP*G)-3' × 1 5'-D(*CP*TP*AP*TP*CP*TP*GP*AP*GP*TP*AP*TP*T)-3' × 1 PG4 TETRAETHYLENE GLYCOL × 1 GOL GLYCEROL × 3 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 6.5;298 K;PEG 20000, pH 6.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K Resolution 2.50 Å R-free 0.272

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 3
Chains and sequence ranges Author chain A; PDBConstruct 1–351; UniProt 1–351 Author chain B; 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 1sxp

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id1sxp
Deposition date deposition_date2004-03-31
Structure title titleBGT in complex with a 13mer DNA containing a central A:G mismatch
Keywords keywordsflipped-out base, TRANSFERASE-DNA COMPLEX; TRANSFERASE/DNA
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier30.90
Radius of gyration Rg (electron density) rg_electron30.72
Forward intensity I(0) i0129403000.00
Molecular weight molecular_weight89148.0 kDa
Excluded volume excluded_volume111130 ų
Envelope volume envelope_volume139230 ų
Hydration-shell volume shell_volume38081 ų
Envelope diameter envelope_diameter99.9
Shell Rg shell_rg37.56
Envelope Rg envelope_rg30.07
Shape Rg shape_rg30.71
Total Rg total_rg31.34
Total atoms total_atoms6259
Residues n_residues726
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 dmax98.2
Rg (real space) rg_real30.86
Rg uncertainty (real space) rg_real_error0.79
I(0) (real space) i0_real1.2940e+08
I(0) uncertainty (real space) i0_real_error2.0210e+06
Rg (reciprocal space) rg_reciprocal30.88
I(0) (reciprocal space) i0_reciprocal129400000.0000
Solution quality estimate total_estimate0.9039
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary32.7
Skewness Skewness skewness0.273
Kurtosis Kurtosis kurtosis-0.551
Angular range angular_range— – 0.2550 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha22870000.0000
Real-space data points n_real_points52
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.935; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.950

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

7. Fold Classification (SCOP + CATH) 6 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd1sxpa_
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)
Domain ID domain_idd1sxpb_
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)

CATH v4.4 (4 domains)

Domain ID domain_id1sxpA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2000 — Glycogen Phosphorylase B;
Domain ID domain_id1sxpA02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2000 — Glycogen Phosphorylase B;
Domain ID domain_id1sxpB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2000 — Glycogen Phosphorylase B;
Domain ID domain_id1sxpB02
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily2000 — Glycogen Phosphorylase B;

8. Citations (1)

9. Files and Curves (10)