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Crystal structure of ttr variant I84S in complex with CHF5074 at acidic pH

Analyse Crystal structure of ttr variant I84S in complex with CHF5074 at acidic pH in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4I87
Type: protein
Length: 231 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Ligands: H50
Pockets: 2 · best druggability 0.35

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transthyretin	protein	116	6% helix, 53% strand	P02766
B	Transthyretin	protein	115	6% helix, 51% strand	P02766

Ligands and binding sites

H50 · 1-(3',4'-dichloro-2-fluorobiphenyl-4-yl) cyclopropanecarboxylic acid · ligand · 2 copies · chains A, B

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	81	0.35	0.75	20	empty
2	76	0.34	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 909 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

4I87 · Crystal structure of TTR variant I84S in complex with CHF5074 at acidic pH · 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 4I87 · PDBe 4I87 · UniProt P02766

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