3e3e

Human Thioredoxin Double Mutant C35S,C73R

Method: X-RAY DIFFRACTION Dmax: 63.8 Å Quality: GOOD

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

Thioredoxin

Homo sapiens

UniProt P10599

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 1–105 Mutation:C35S, C73R P6G HEXAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;292 K;0.1 M Na acetate, pH 4.6, and 30 % (v/v) PEG 300, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.01 Å R-free 0.261
2 Protein monomer Monomer Protein × 1 PDB declaration: monomeric(1) Consistent with protein copy count Chain B; UniProt 1–105 Mutation:C35S, C73R P6G HEXAETHYLENE GLYCOL × 1 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 4.6;292 K;0.1 M Na acetate, pH 4.6, and 30 % (v/v) PEG 300, VAPOR DIFFUSION, SITTING DROP, temperature 292K Resolution 2.01 Å R-free 0.261

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.

34 other PDB entries and 58 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name THIO_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–105; UniProt 1–105 Author chain B; PDBConstruct 1–105; UniProt 1–105

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 3e3e

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 3e3e
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2. Structure Basics 2. Structure Basics

Entry ID entry_id3e3e
Deposition date deposition_date2008-08-07
Structure title titleHuman Thioredoxin Double Mutant C35S,C73R
Keywords keywordsElectron Transport, Phosphoprotein, Redox-active center; ELECTRON TRANSPORT
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.95
Radius of gyration Rg (electron density) rg_electron18.85
Forward intensity I(0) i09867480.00
Molecular weight molecular_weight23839.0 kDa
Excluded volume excluded_volume30046 ų
Envelope volume envelope_volume35437 ų
Hydration-shell volume shell_volume16383 ų
Envelope diameter envelope_diameter65.0
Shell Rg shell_rg24.15
Envelope Rg envelope_rg18.81
Shape Rg shape_rg18.79
Total Rg total_rg19.88
Total atoms total_atoms1672
Residues n_residues210
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 dmax63.8
Rg (real space) rg_real19.94
Rg uncertainty (real space) rg_real_error0.33
I(0) (real space) i0_real9.8670e+06
I(0) uncertainty (real space) i0_real_error1.1840e+05
Rg (reciprocal space) rg_reciprocal19.94
I(0) (reciprocal space) i0_reciprocal9867000.0000
Solution quality estimate total_estimate0.8818
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.4
Skewness Skewness skewness0.307
Kurtosis Kurtosis kurtosis-0.485
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2477000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.884; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.977; Smooth: 0.831

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (3)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3e3ea_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.1 — Thioltransferase
Domain ID domain_idd3e3eb_
Class classc — Alpha and beta proteins (a/b)
Fold Fold foldc.47 — Thioredoxin fold
Superfamily Superfamily superfamilyc.47.1 — Thioredoxin-like
Family Family familyc.47.1.1 — Thioltransferase

CATH v4.4 (2 domains)

Domain ID domain_id3e3eA00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin
Domain ID domain_id3e3eB00
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology30 — Glutaredoxin
Homologous superfamily homologous superfamily10 — Glutaredoxin

8. Citations (1)

9. Files and Curves (10)