← Back to search
8uqv

Trehalose Synthase (TreS) of Mycobacterium tuberculosis in complex with 6-TreAz compound

Method: ELECTRON MICROSCOPY Dmax: 136.4 Å Quality: EXCELLENT
▼

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

Trehalose synthase/amylase TreS

Mycobacterium tuberculosis

UniProt P9WQ18

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 × 4 PDB declaration: tetrameric（4） Consistent with protein copy count Chain A； UniProt 12–586 Chain B； UniProt 12–586 Chain C； UniProt 12–586 Chain D； UniProt 12–586 Fragment：residues 12-586 GLC alpha-D-glucopyranose × 4 XVC 6-azido-6-deoxy-alpha-D-glucopyranose × 4 CA CALCIUM ION × 4 ELECTRON MICROSCOPY cryo-EM buffer：pH 7.5；50 mM Tris pH 7.5, 300 mM NaCl and 0.3 mM TCEP cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.60 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 8UQV Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
8UZH SUMO fused Trehalose Synthase (TreS) of Mycobacterium tuberculosis Deposited 2023-11-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics Assembly 1 Insufficient information Homooligomer；Protein × 4 PDB declaration: tetrameric
Chain A 13–601（589 aa）
Chain B 13–601（589 aa）
Not recorded CA CALCIUM ION × 6 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP；289 K；0.8 M Ammonium sulfate, 0.1 M Sodium Citrate pH 5.0
Resolution 2.80 Å R-free 0.290

1 other PDB entries and 1 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TRES_MYCTO
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–575； UniProt 12–586 Author chain B； PDBConstruct 1–575； UniProt 12–586 Author chain C； PDBConstruct 1–575； UniProt 12–586 Author chain D； PDBConstruct 1–575； UniProt 12–586

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 8uqv

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8uqv
Download Download
▼

2. Structure Basics 2. Structure Basics

Entry ID entry_id8uqv
Deposition date deposition_date2023-10-24
Structure title titleTrehalose Synthase (TreS) of Mycobacterium tuberculosis in complex with 6-TreAz compound
Keywords keywordsTreS, Trehalose Synthase, Mycobacterium tuberculosis, 6-TreAz, CYTOSOLIC PROTEIN; CYTOSOLIC PROTEIN
Experimental Method methodELECTRON MICROSCOPY
▼

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

Radius of gyration Rg (Guinier) rg_guinier43.64 Å
Radius of gyration Rg (electron density) rg_electron42.89 Å
Forward intensity I(0) i0935257000.00
Molecular weight molecular_weight253460.0 kDa
Excluded volume excluded_volume316350 ų
Envelope volume envelope_volume411120 ų
Hydration-shell volume shell_volume76660 ų
Envelope diameter envelope_diameter133.3 Å
Shell Rg shell_rg50.51 Å
Envelope Rg envelope_rg42.40 Å
Shape Rg shape_rg42.90 Å
Total Rg total_rg43.15 Å
Total atoms total_atoms18028
Residues n_residues2188
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
▼

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

Maximum dimension Dmax dmax136.4 Å
Rg (real space) rg_real43.44 Å
Rg uncertainty (real space) rg_real_error0.98 Å
I(0) (real space) i0_real9.3530e+08
I(0) uncertainty (real space) i0_real_error1.5930e+07
Rg (reciprocal space) rg_reciprocal43.64 Å
I(0) (reciprocal space) i0_reciprocal935500000.0000
Solution quality estimate total_estimate0.9073
Solution quality rating solution_quality EXCELLENT a EXCELLENT solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary56.8 Å
Skewness Skewness skewness0.104
Kurtosis Kurtosis kurtosis-0.696
Angular range angular_range— – 0.1800 Å−1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha317400000.0000
Real-space data points n_real_points37
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.949; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.951
▶

5. Crystallography and Experiment 5. Crystallography & Experiment

▶

6. Entities and Polymers Entities & Polymers (5)

▶

8. Citations (1)

▶

9. Files and Curves (10)