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6scj

The structure of human thyroglobulin

Method: ELECTRON MICROSCOPY Dmax: 230.0 Å Quality: GOOD
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1. Protein Identity and Related Structures Protein Identity & Related Structures

Thyroglobulin

Homo sapiens

UniProt P01266

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Other combination Homooligomer Protein × 2 其他Polymer 2 PDB declaration: dimeric（2） Consistent with protein copy count Chain A； UniProt 1–2768 Chain B； UniProt 1–2768 Not recorded beta-D-mannopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose × 2 NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 30 ELECTRON MICROSCOPY cryo-EM buffer：pH 8；TRIS 0.05M, 0.2M NaCl pH 8 cryo-EM vitrification conditions：Cryogen ETHANE Resolution 3.60 Å

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.

Other PDB Difference from Current Entry 6SCJ Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Method and Experimental Conditions Structure Quality
7B75 Cryo-EM Structure of Human Thyroglobulin Deposited 2020-12-09 Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Homooligomer；Protein × 2 PDB declaration: dimeric
Chain A 1–2768（2768 aa）
Chain B 1–2768（2768 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 16 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5；0.22 um filtered and degased
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.20 Å
9I0O Cryo-EM structure of human sortilin ectodomain in complex with a thyroglobulin C-terminal peptide Deposited 2025-01-15 Different construct Different mutation/modification Different oligomeric state Different ligand/ion Different experimental conditions Different structure-quality metrics Assembly 1 Other combination Heteromer；Protein × 2 PDB declaration: dimeric
Chain B 2749–2768（20 aa）
Not recorded NAG 2-acetamido-2-deoxy-beta-D-glucopyranose × 1 ELECTRON MICROSCOPY
cryo-EM buffer pH 7.5
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.36 Å

2 other PDB entries and 2 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name THYG_HUMAN
Isoform —
PDB entities 1
Chains and sequence ranges Author chain A； PDBConstruct 1–2768； UniProt 1–2768 Author chain B； PDBConstruct 1–2768； UniProt 1–2768

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 6scj

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 6scj
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2. Structure Basics 2. Structure Basics

Entry ID entry_id6scj
Deposition date deposition_date2019-07-24
Structure title titleThe structure of human thyroglobulin
Keywords keywordsThyroglobulin, Thyroid, thyroid hormones, Tri-iodo-thyronine, Thyroxine, HORMONE; HORMONE
Experimental Method methodELECTRON MICROSCOPY
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3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier65.43 Å
Radius of gyration Rg (electron density) rg_electron66.03 Å
Forward intensity I(0) i04844200000.00
Molecular weight molecular_weight568700.0 kDa
Excluded volume excluded_volume703750 ų
Envelope volume envelope_volume1144500 ų
Hydration-shell volume shell_volume147570 ų
Envelope diameter envelope_diameter257.5 Å
Shell Rg shell_rg65.43 Å
Envelope Rg envelope_rg65.67 Å
Shape Rg shape_rg65.98 Å
Total Rg total_rg66.18 Å
Total atoms total_atoms39884
Residues n_residues5102
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 Å−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
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4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax230.0 Å
Rg (real space) rg_real65.90 Å
Rg uncertainty (real space) rg_real_error1.78 Å
I(0) (real space) i0_real4.8410e+09
I(0) uncertainty (real space) i0_real_error9.7800e+07
Rg (reciprocal space) rg_reciprocal64.95 Å
I(0) (reciprocal space) i0_reciprocal4835000000.0000
Solution quality estimate total_estimate0.8341
Solution quality rating solution_quality GOOD a GOOD solution
P(r) peaks n_peaks2
Primary peak position r_peak_primary76.7 Å
Skewness Skewness skewness0.640
Kurtosis Kurtosis kurtosis0.253
Angular range angular_range— – 0.1200 Å−1
Current regularization parameter α current_alpha0.0240
Highest regularization parameter α highest_alpha437100000.0000
Real-space data points n_real_points25
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.684; Stabil: 1.000; Sysdev: 1.000; Positv: 1.000; Valcen: 0.999; Smooth: 0.789
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5. Crystallography and Experiment 5. Crystallography & Experiment

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6. Entities and Polymers Entities & Polymers (3)

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7. Fold Classification (SCOP + CATH) 2 domains

CATH v4.4 (2 domains)

Domain ID domain_id6scjA01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain
Domain ID domain_id6scjB01
Class class3 — Alpha Beta
Architecture architecture40 — 3-Layer(aba) Sandwich
Topology topology50 — Rossmann fold
Homologous superfamily homologous superfamily1820 — Alpha/Beta hydrolase fold, catalytic domain
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8. Citations (1)

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9. Files and Curves (10)