4pm1

Human transthyretin (TTR) complexed with 16-alpha-bromo-estradiol

Method: X-RAY DIFFRACTION Dmax: 58.7 Å Quality: GOOD

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

Transthyretin

OrganismNot specified

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 ESZ (14beta,16alpha,17alpha)-16-bromoestra-1,3,5(10)-triene-3,17-diol × 4 EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION X-ray crystallization conditions:VAPOR DIFFUSION, SITTING DROP;pH 6.2;293 K;Protein: 5 mg/ml TTR dialysed against 0.1 M NaCl, 0.05M Na acetate, pH 5.5. Precipitant:: 70% (30% PEG 4000, 0.2M imidazole malate, pH 6.0) 30% (18% monomethyl PEG 2000, 0.1 M sodium cacodylate, pH 6.5). Cryoprotectant: 40% (25 % diethylene glycol + 12.5 % MPD + 37.5 % 2,3-butanediol + 12.5 % 1,4-dioxane) 50% (12.5% MPEG 5K, 25% MPEG 550) 0.1 M (mixed Na propionate, Na cacodylate, Bis-Tris-propane 50% at pH 4.0 and 50% pH 9.5) Resolution 1.23 Å R-free 0.211

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 4pm1

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 4pm1
Download Download

2. Structure Basics 2. Structure Basics

Entry ID entry_id4pm1
Deposition date deposition_date2014-05-20
Structure title titleHuman transthyretin (TTR) complexed with 16-alpha-bromo-estradiol
Keywords keywordsHuman transthyretin hydrophobic ligand solubilization, Thyroid hormone-binding protein; Thyroid hormone-binding protein
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier18.79
Radius of gyration Rg (electron density) rg_electron17.47
Forward intensity I(0) i011829600.00
Molecular weight molecular_weight26193.0 kDa
Excluded volume excluded_volume32963 ų
Envelope volume envelope_volume37335 ų
Hydration-shell volume shell_volume17810 ų
Envelope diameter envelope_diameter62.0
Shell Rg shell_rg23.63
Envelope Rg envelope_rg17.68
Shape Rg shape_rg17.44
Total Rg total_rg18.52
Total atoms total_atoms1844
Residues n_residues232
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 dmax58.7
Rg (real space) rg_real18.68
Rg uncertainty (real space) rg_real_error0.36
I(0) (real space) i0_real1.1830e+07
I(0) uncertainty (real space) i0_real_error1.4000e+05
Rg (reciprocal space) rg_reciprocal18.70
I(0) (reciprocal space) i0_reciprocal11830000.0000
Solution quality estimate total_estimate0.8023
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks3
Primary peak position r_peak_primary21.7
Skewness Skewness skewness0.148
Kurtosis Kurtosis kurtosis-0.393
Angular range angular_range— – 0.4250 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha2723000.0000
Real-space data points n_real_points74
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.827; Stabil: 0.984; Sysdev: 1.000; Positv: 1.000; Valcen: 0.993; Smooth: 0.000

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (4)

7. Fold Classification (SCOP + CATH) 4 domains

SCOP 2.08 (2 domains)

Domain ID domain_idd4pm1a_
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_idd4pm1b_
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_id4pm1A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily180 — Transthyretin/hydroxyisourate hydrolase domain
Domain ID domain_id4pm1B00
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)