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The structure of human thyroglobulin

Analyse The structure of human thyroglobulin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6SCJ
Type: protein
Length: 5,102 residues
Chains: 2
Method: electron microscopy
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Thyroglobulin
UniProt: P01266
Ligands: NAG, BMA
Pockets: 20 · best druggability 0.85

Structure

electron microscopy · 1 distinct chain · 22% helix, 16% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Thyroglobulin	protein	2551	22% helix, 16% strand	P01266

Ligands and binding sites

NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 34 copies · chains A, B
BMA · beta-D-mannopyranose · sugar · 2 copies · chains B, A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

20 pockets found on a 1 Å grid, 20 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	1130	0.85	0.86	107	empty
2	1153	0.85	0.86	97	empty
3	990	0.82	0.83	84	empty
4	1180	0.81	0.82	84	empty
5	712	0.79	0.84	71	empty

Interfaces

1 interface between chains.

A–B · 10881 Å² buried · 96 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 120 disulfide, 32 glycan (disulfide, N-glycosylation).

Compared structures

6SCJ · The structure of human thyroglobulin · the same entry in another collection · chain A against A, TM-score 1.00

Analyse

Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
Every structure of UniProt P01266
Elsewhere: RCSB PDB 6SCJ · PDBe 6SCJ · UniProt P01266

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