1bze

TERTIARY STRUCTURES OF THREE AMYLOIDOGENIC TRANSTHYRETIN VARIANTS AND IMPLICATIONS FOR AMYLOID FIBRIL FORMATION

Method: X-RAY DIFFRACTION Dmax: 68.4 Å Quality: GOOD

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

PROTEIN (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 Mutation:M119T No other associated polymer X-RAY DIFFRACTION X-ray crystallization conditions:pH 5.5;PURIFIED PROTEIN (10MG/ML IN TRIS BUFFER, PH 7.5) WAS CRYSTALLIZED FROM 2M AMMONIUM SULFATE, 100MM CITRATE BUFFER, PH 5.5 AT ROOM TEMPERATURE. Resolution 1.80 Å R-free 0.273

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 1bze

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 1bze
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2. Structure Basics 2. Structure Basics

Entry ID entry_id1bze
Deposition date deposition_date1998-10-28
Structure title titleTERTIARY STRUCTURES OF THREE AMYLOIDOGENIC TRANSTHYRETIN VARIANTS AND IMPLICATIONS FOR AMYLOID FIBRIL FORMATION
Keywords keywordsTHYROID HORMONE, LIVER, PLASMA, CEREBROSPINAL FLUID, POLYNEUROPATHY, DISEASE MUTATION, TRANSPORT, THYROXINE, BINDING PROTEIN; BINDING PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier19.90
Radius of gyration Rg (electron density) rg_electron18.59
Forward intensity I(0) i013490700.00
Molecular weight molecular_weight27573.0 kDa
Excluded volume excluded_volume34524 ų
Envelope volume envelope_volume40039 ų
Hydration-shell volume shell_volume18279 ų
Envelope diameter envelope_diameter67.9
Shell Rg shell_rg24.61
Envelope Rg envelope_rg18.82
Shape Rg shape_rg18.55
Total Rg total_rg19.64
Total atoms total_atoms1946
Residues n_residues254
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 dmax68.4
Rg (real space) rg_real19.83
Rg uncertainty (real space) rg_real_error0.41
I(0) (real space) i0_real1.3490e+07
I(0) uncertainty (real space) i0_real_error1.6160e+05
Rg (reciprocal space) rg_reciprocal19.84
I(0) (reciprocal space) i0_reciprocal13490000.0000
Solution quality estimate total_estimate0.8633
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary22.2
Skewness Skewness skewness0.276
Kurtosis Kurtosis kurtosis-0.243
Angular range angular_range— – 0.4000 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2769000.0000
Real-space data points n_real_points72
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.758; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.979; Smooth: 0.965

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_idd1bzea_
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_idd1bzeb_
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_id1bzeA00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily180 — Transthyretin/hydroxyisourate hydrolase domain
Domain ID domain_id1bzeB00
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)