5fw8

Structure of human transthyretin mutant E89K

Method: X-RAY DIFFRACTION Dmax: 96.0 Å Quality: REASONABLE

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 Mutation:YES No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.60 Å R-free 0.204
2 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:YES No other associated polymer X-RAY DIFFRACTION mmCIF provides none of the parsed experimental conditions Resolution 1.60 Å R-free 0.204

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 500 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 5fw8

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 5fw8
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2. Structure Basics 2. Structure Basics

Entry ID entry_id5fw8
Deposition date deposition_date2016-02-12
Structure title titleStructure of human transthyretin mutant E89K
Keywords keywordsTRANSPORT PROTEIN, T4-BINDING, T4-BINDING PROTEIN NON-AMYLOIDOGENIC; TRANSPORT PROTEIN
Experimental Method methodX-RAY DIFFRACTION

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

Radius of gyration Rg (Guinier) rg_guinier31.93
Radius of gyration Rg (electron density) rg_electron31.79
Forward intensity I(0) i09954470.00
Molecular weight molecular_weight25337.0 kDa
Excluded volume excluded_volume31904 ų
Envelope volume envelope_volume45523 ų
Hydration-shell volume shell_volume12407 ų
Envelope diameter envelope_diameter99.3
Shell Rg shell_rg37.65
Envelope Rg envelope_rg30.62
Shape Rg shape_rg31.79
Total Rg total_rg32.39
Total atoms total_atoms1792
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 dmax96.0
Rg (real space) rg_real32.42
Rg uncertainty (real space) rg_real_error0.86
I(0) (real space) i0_real9.9540e+06
I(0) uncertainty (real space) i0_real_error1.4910e+05
Rg (reciprocal space) rg_reciprocal32.22
I(0) (reciprocal space) i0_reciprocal9953000.0000
Solution quality estimate total_estimate0.5783
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary17.3
Skewness Skewness skewness0.295
Kurtosis Kurtosis kurtosis-1.141
Angular range angular_range— – 0.2500 −1
Current regularization parameter α current_alpha0.0000
Highest regularization parameter α highest_alpha585800.0000
Real-space data points n_real_points51
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.147; Stabil: 0.998; Sysdev: 1.000; Positv: 1.000; Valcen: 0.074; Smooth: 0.005

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_idd5fw8a_
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_idd5fw8b_
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_id5fw8A00
Class class2 — Mainly Beta
Architecture architecture60 — Sandwich
Topology topology40 — Immunoglobulin-like
Homologous superfamily homologous superfamily180 — Transthyretin/hydroxyisourate hydrolase domain
Domain ID domain_id5fw8B00
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)