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Human transthyretin (ttr) complexed with (E)-3-(((4- HYDROXYBENZYLIDENE)AMINO)OXY)PROPANOIC acid

Analyse Human transthyretin (ttr) complexed with (E)-3-(((4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 6TJN
Type: protein
Length: 232 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Ligands: NEK
Pockets: 2 · best druggability 0.31

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

NEK · 3-[(~{E})-(4-hydroxyphenyl) methylideneamino]oxypropanoic 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	77	0.31	0.74	16	empty
2	65	0.29	0.73	19	empty

Interfaces

1 interface between chains.

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

Compared structures

6TJN · Human transthyretin (TTR) complexed with (E)-3-(((4-hydroxybenzylidene)amino)oxy)propanoic… · 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 6TJN · PDBe 6TJN · UniProt P02766

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