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Human transthyretin (ttr) complexed with 2-((3,5-dichloro-4- HYDROXYPHENYL)AMINO)BENZOIC acid

Analyse Human transthyretin (ttr) complexed with 2-((3,5-dichloro-4… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3M1O
Type: protein
Length: 226 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Ligands: CJZ
Pockets: 1 · best druggability 0.31

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transthyretin	protein	115	6% helix, 53% strand	P02766
B	Transthyretin	protein	111	6% helix, 53% strand	P02766

Ligands and binding sites

CJZ · 2-[(3,5-dichloro-4-hydroxyphenyl)amino]benzoic acid · ligand · 2 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	67	0.31	0.74	16	empty

Interfaces

1 interface between chains.

A–B · 941 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

3M1O · Human Transthyretin (TTR) complexed with 2-((3,5-dichloro-4-hydroxyphenyl)amino)benzoic… · 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 3M1O · PDBe 3M1O · UniProt P02766

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