9xub

Crystal Structure of Thioredoxin reductase from Mycobacterium tuberculosis.

Method: X-RAY DIFFRACTION Dmax: 111.9 Å Quality: GOOD

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

Thioredoxin reductase

Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh)

UniProt P9WHH0

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 14–321 Chain B; UniProt 14–321 Not recorded FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.2;294 K;0.2 M Ammonium nitrate PH 6.2,20% w/v Polyethylene glycol 3350 Resolution 2.60 Å R-free 0.232
2 Protein homooligomer Homooligomer Protein × 2 PDB declaration: dimeric(2) Consistent with protein copy count Chain C; UniProt 14–321 Chain D; UniProt 14–321 Not recorded FAD FLAVIN-ADENINE DINUCLEOTIDE × 2 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.2;294 K;0.2 M Ammonium nitrate PH 6.2,20% w/v Polyethylene glycol 3350 Resolution 2.60 Å R-free 0.232

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.

No other PDB entry for the same UniProt protein was found.

View Construct and Data Evidence
UniProt name TRXB_MYCTO
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 2–309; UniProt 14–321 Author chain B; PDBConstruct 2–309; UniProt 14–321 Author chain C; PDBConstruct 2–309; UniProt 14–321 Author chain D; PDBConstruct 2–309; UniProt 14–321

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 9xub

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 9xub
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2. Structure Basics 2. Structure Basics

Entry ID entry_id9xub
Deposition date deposition_date2025-11-24
Structure title titleCrystal Structure of Thioredoxin reductase from Mycobacterium tuberculosis.
Keywords keywordsThioredoxin reductase, Mycobacterium tuberculosis, OXIDOREDUCTASE; OXIDOREDUCTASE
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier33.70
Radius of gyration Rg (electron density) rg_electron33.22
Forward intensity I(0) i0258758000.00
Molecular weight molecular_weight123310.0 kDa
Excluded volume excluded_volume151850 ų
Envelope volume envelope_volume189790 ų
Hydration-shell volume shell_volume46938 ų
Envelope diameter envelope_diameter122.5
Shell Rg shell_rg40.54
Envelope Rg envelope_rg33.36
Shape Rg shape_rg33.22
Total Rg total_rg33.71
Total atoms total_atoms8660
Residues n_residues1136
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 dmax111.9
Rg (real space) rg_real33.69
Rg uncertainty (real space) rg_real_error0.87
I(0) (real space) i0_real2.5880e+08
I(0) uncertainty (real space) i0_real_error4.1820e+06
Rg (reciprocal space) rg_reciprocal33.70
I(0) (reciprocal space) i0_reciprocal258800000.0000
Solution quality estimate total_estimate0.8865
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary38.1
Skewness Skewness skewness0.348
Kurtosis Kurtosis kurtosis-0.359
Angular range angular_range— – 0.2350 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha98400000.0000
Real-space data points n_real_points48
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.868; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.937

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

8. Citations (1)

9. Files and Curves (10)