Research workbench

Crystal structure of human transthyretin in complex with tetrabromobisphenol a (tbbpa)

Analyse Crystal structure of human transthyretin in complex with tetrabromobisphenol a… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5HJG
Type: protein
Length: 232 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Ligands: XDI, NA
Pockets: 2 · best druggability 0.32

Structure

x-ray diffraction · 1 distinct chain · 6% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Transthyretin	protein	116	6% helix, 53% strand	P02766

Ligands and binding sites

XDI · 4,4'-propane-2,2-diylbis(2,6-dibromophenol) · ligand · 2 copies · chains A, B
NA · Sodium ion · metal · chains A

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

Pockets

2 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	50	0.32	0.77	14	empty
2	60	0.30	0.75	16	empty

Interfaces

1 interface between chains.

A–B · 933 Å² buried · 19 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 1 covalent (covalent ligand).

Compared structures

5HJG · Crystal Structure of Human Transthyretin in Complex with Tetrabromobisphenol A (TBBPA) · 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 5HJG · PDBe 5HJG · UniProt P02766

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.