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Crystal structure of human transthyretin in complex with 1-amino-5-naphthalene sulfonate

Analyse Crystal structure of human transthyretin in complex with 1-amino-5-naphthalene… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3CFT
Type: protein
Length: 231 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 1.87
Source: Homo sapiens
Molecule: Transthyretin
UniProt: P02766
Ligands: 5NS
Pockets: 1 · best druggability 0.33

Structure

x-ray diffraction · resolution 1.87 · 2 distinct chains · 6% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transthyretin	protein	116	5% helix, 53% strand	P02766
B	Transthyretin	protein	115	6% helix, 53% strand	P02766

Ligands and binding sites

5NS · 5-aminonaphthalene-1-sulfonic acid · ligand · 3 copies · chains A, B

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

Pockets

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

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	86	0.33	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 942 Å² buried · 19 hydrogen bonds · protein-protein

Compared structures

3CFT · Crystal structure of human transthyretin in complex with 1- amino-5-naphthalene sulfonate · 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 3CFT · PDBe 3CFT · UniProt P02766

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