MolNFT v1 · #106800 · protein

Human transthyretin (ttr) complexed with 3-(9H-fluoren-9- YLIDENEAMINOOXY)ETHANOIC acid

4TQH: “Human transthyretin (ttr) complexed with 3-(9H-fluoren-9- YLIDENEAMINOOXY)ETHANOIC acid”. X-ray diffraction, 1 ligand (ES8), 2 pockets (best druggability 0.30). MolNFT v1 #106800 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 4TQH
Type: protein
Length: 234 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Ligands: ES8
Pockets: 2 · best druggability 0.30

Structure

x-ray diffraction · 1 distinct chain · 5% helix, 52% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, B	Transthyretin	protein	117	5% helix, 52% strand	P02766

Ligands and binding sites

ES8 · [(9H-fluoren-9-ylideneamino)oxy]acetic acid · ligand · 2 copies · chains A, B
EDO · 1,2-ethanediol · additive · 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	51	0.30	0.76	13	empty
2	58	0.30	0.76	15	empty

Interfaces

1 interface between chains.

A–B · 932 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

4TQH · Human transthyretin (TTR) complexed with 3-(9H-fluoren-9-ylideneaminooxy)ethanoic acid · 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 4TQH · PDBe 4TQH · UniProt P02766

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