3tfb

Transthyretin natural mutant A25T

Method: X-RAY DIFFRACTION Dmax: 59.0 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 30–145 Chain B; UniProt 30–145 Fragment:UNP residues 30-145 Mutation:A45T No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, HANGING DROP;pH 7.5;291 K;100 mM HEPES, 200 mM CaCl2 and 28% PEG400, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K Resolution 2.03 Å R-free 0.239

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 1–116; UniProt 30–145 Author chain B; PDBConstruct 1–116; UniProt 30–145

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 3tfb

P(r) Distance Distribution P(r) Distribution

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

Entry ID entry_id3tfb
Deposition date deposition_date2011-08-15
Structure title titleTransthyretin natural mutant A25T
Keywords keywordsTransthyretin, Immunoglobulin-like, Transport Protein, extracellular, HORMONE-BINDING PROTEIN, HORMONE 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_guinier18.75
Radius of gyration Rg (electron density) rg_electron17.41
Forward intensity I(0) i010981800.00
Molecular weight molecular_weight25055.0 kDa
Excluded volume excluded_volume31481 ų
Envelope volume envelope_volume35943 ų
Hydration-shell volume shell_volume17323 ų
Envelope diameter envelope_diameter60.0
Shell Rg shell_rg23.43
Envelope Rg envelope_rg17.55
Shape Rg shape_rg17.38
Total Rg total_rg18.46
Total atoms total_atoms1772
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 dmax59.0
Rg (real space) rg_real18.63
Rg uncertainty (real space) rg_real_error0.31
I(0) (real space) i0_real1.0980e+07
I(0) uncertainty (real space) i0_real_error1.2540e+05
Rg (reciprocal space) rg_reciprocal18.65
I(0) (reciprocal space) i0_reciprocal10980000.0000
Solution quality estimate total_estimate0.8946
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary21.8
Skewness Skewness skewness0.125
Kurtosis Kurtosis kurtosis-0.451
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2518000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.886; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.991; Smooth: 0.975

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (2)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd3tfba_
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_idd3tfbb_
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_id3tfbA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily180 — Transthyretin/hydroxyisourate hydrolase domain
Domain ID domain_id3tfbB00
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)