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Structure of human transthyretin LEU55PRO mutant in complex with tafamidis

Analyse Structure of human transthyretin LEU55PRO mutant in complex with tafamidis in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6E74
Type: protein
Length: 230 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Ligands: 3MI
Pockets: 2 · best druggability 0.31

Structure

x-ray diffraction · 1 distinct chain · 7% helix, 50% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Transthyretin	protein	115	7% helix, 50% strand	P02766

Ligands and binding sites

3MI · 2-(3,5-dichlorophenyl)-1,3-benzoxazole-6-carboxylic 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	60	0.31	0.76	14	empty
2	51	0.31	0.77	13	empty

Interfaces

1 interface between chains.

A–B · 938 Å² buried · 21 hydrogen bonds · protein-protein

Compared structures

6E74 · Structure of Human Transthyretin Leu55Pro Mutant in Complex with Tafamidis · 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 6E74 · PDBe 6E74 · UniProt P02766

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