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Human transthyretin (also called prealbumin) complex with 3, 3',5,5'- tetraiodothyroacetic acid (T4AC)

Analyse Human transthyretin (also called prealbumin) complex with 3, 3',5,5'… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1Z7J
Type: protein
Length: 234 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Ligands: T4A
Pockets: 3 · best druggability 0.40

Structure

x-ray diffraction · 2 distinct chains · 5% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transthyretin	protein	116	5% helix, 53% strand	P02766
B	Transthyretin	protein	118	5% helix, 52% strand	P02766

Ligands and binding sites

T4A · 3,3',5,5'-tetraiodothyroacetic acid · ligand · 2 copies · chains A, B

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

Pockets

3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	53	0.40	0.82	16	empty
2	67	0.33	0.76	16	empty
3	59	0.32	0.76	13	empty

Interfaces

1 interface between chains.

A–B · 919 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

1Z7J · Human transthyretin (also called prealbumin) complex with 3, 3',5,5'-tetraiodothyroacetic… · 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 P02766
Elsewhere: RCSB PDB 1Z7J · PDBe 1Z7J · UniProt P02766

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