5ayt

Crystal structure of transthyretin in complex with L6

Method: X-RAY DIFFRACTION Dmax: 65.2 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 1–147 Chain B; UniProt 1–147 Not recorded L6Y 2-oxidanyl-6-(phenylcarbonyl)benzo[de]isoquinoline-1,3-dione × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7;293 K;18% polyethylene glycol 400, 0.1 M HEPES-NaOH, 0.2 M CaCl2, 1 mM L6 Resolution 1.40 Å R-free 0.209

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 13–159; UniProt 1–147 Author chain B; PDBConstruct 13–159; UniProt 1–147

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 5ayt

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5ayt
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5ayt
Deposition date deposition_date2015-09-03
Structure title titleCrystal structure of transthyretin in complex with L6
Keywords keywordsAmyloidogenic protein, Inhibitor, Stabilizer, Drug discovery, TRANSPORT PROTEIN-INHIBITOR complex; TRANSPORT PROTEIN/INHIBITOR
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.87
Radius of gyration Rg (electron density) rg_electron17.47
Forward intensity I(0) i011507900.00
Molecular weight molecular_weight25775.0 kDa
Excluded volume excluded_volume32393 ų
Envelope volume envelope_volume37094 ų
Hydration-shell volume shell_volume17722 ų
Envelope diameter envelope_diameter61.5
Shell Rg shell_rg23.63
Envelope Rg envelope_rg17.64
Shape Rg shape_rg17.43
Total Rg total_rg18.55
Total atoms total_atoms1826
Residues n_residues230
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 dmax65.2
Rg (real space) rg_real18.75
Rg uncertainty (real space) rg_real_error0.52
I(0) (real space) i0_real1.1510e+07
I(0) uncertainty (real space) i0_real_error1.4610e+05
Rg (reciprocal space) rg_reciprocal18.77
I(0) (reciprocal space) i0_reciprocal11510000.0000
Solution quality estimate total_estimate0.7858
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary22.6
Skewness Skewness skewness0.130
Kurtosis Kurtosis kurtosis-0.457
Angular range angular_range— – 0.4200 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha3100000.0000
Real-space data points n_real_points73
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.738; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.997; 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_idd5ayta_
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_idd5aytb_
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_id5aytA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily180 — Transthyretin/hydroxyisourate hydrolase domain
Domain ID domain_id5aytB00
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)