3tct

Structure of wild-type TTR in complex with tafamidis

Method: X-RAY DIFFRACTION Dmax: 60.3 Å Quality: GOOD

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

Transthyretin

Homo sapiens

UniProt P02766

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 21–147 Chain B; UniProt 21–147 Fragment:unp residues 21-147 3MI 2-(3,5-dichlorophenyl)-1,3-benzoxazole-6-carboxylic acid × 4 X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;THE WT-TTR WAS CONCENTRATED TO 4 MG/ML IN 10 MM NAPI, 100 MM KCL, AT PH 7.6 AND CO-CRYSTALLIZED AT ROOM TEMPERATURE WITH INHIBITORS USING THE VAPOR-DIFFUSION SITTING DROP METHOD, CRYSTALS WERE GROWN FROM 1.395 M SODIUM CITRATE, 3.5% V/V GLYCEROL AT PH 5.5. THE CRYSTALS WERE FROZEN USING A CRYO-PROTECTANT SOLUTION OF 1.395 M SODIUM CITRATE, PH 5.5, CONTAINING 10% V/V GLYCEROL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298.0K Resolution 1.30 Å R-free 0.192

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.

460 other PDB entries and 501 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name TTHY_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain A; PDBConstruct 1–127; UniProt 21–147 Author chain B; PDBConstruct 1–127; UniProt 21–147

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 3tct

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3tct
Deposition date deposition_date2011-08-09
Structure title titleStructure of wild-type TTR in complex with tafamidis
Keywords keywords;AMYLOID, AMYLOIDOSIS, DISEASE MUTATION, GAMMA-CARBOXYGLUTAMIC ACID, GLYCOPROTEIN, HORMONE, NEUROPATHY, SECRETED, THYROID HORMONE, TRANSPORT, Kinetic Stabilizer, Inhibition of the Amyloid Cascade, BINDING PROTEIN ;; HORMONE, BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.85
Radius of gyration Rg (electron density) rg_electron17.46
Forward intensity I(0) i011481300.00
Molecular weight molecular_weight25562.0 kDa
Excluded volume excluded_volume32065 ų
Envelope volume envelope_volume36788 ų
Hydration-shell volume shell_volume17598 ų
Envelope diameter envelope_diameter62.4
Shell Rg shell_rg23.62
Envelope Rg envelope_rg17.70
Shape Rg shape_rg17.43
Total Rg total_rg18.50
Total atoms total_atoms1807
Residues n_residues229
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 dmax60.3
Rg (real space) rg_real18.74
Rg uncertainty (real space) rg_real_error0.43
I(0) (real space) i0_real1.1480e+07
I(0) uncertainty (real space) i0_real_error1.6400e+05
Rg (reciprocal space) rg_reciprocal18.75
I(0) (reciprocal space) i0_reciprocal11480000.0000
Solution quality estimate total_estimate0.8094
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.6
Skewness Skewness skewness0.159
Kurtosis Kurtosis kurtosis-0.371
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3021000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.842; Stabil: 0.999; Sysdev: 1.000; Positv: 1.000; Valcen: 0.996; Smooth: 0.000

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_idd3tcta_
Class classb — All beta proteins
Fold Fold foldb.3 — Prealbumin-like
Superfamily Superfamily superfamilyb.3.4 — Transthyretin (synonym: prealbumin)
Family Family familyb.3.4.1 — Transthyretin (synonym: prealbumin)
Domain ID domain_idd3tctb_
Class classb — All beta proteins
Fold Fold foldb.3 — Prealbumin-like
Superfamily Superfamily superfamilyb.3.4 — Transthyretin (synonym: prealbumin)
Family Family familyb.3.4.1 — Transthyretin (synonym: prealbumin)

CATH v4.4 (2 domains)

Domain ID domain_id3tctA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily180 — Transthyretin/hydroxyisourate hydrolase domain
Domain ID domain_id3tctB00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily180 — Transthyretin/hydroxyisourate hydrolase domain

8. Citations (1)

9. Files and Curves (10)