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Crystal structure of human transthyretin in complex with 4-chloro-9, 10-dioxo-9,10-dihydroanthracene-2-carboxylic acid

Analyse Crystal structure of human transthyretin in complex with 4-chloro-9… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7DT3
Type: protein
Length: 229 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Ligands: HG6, CA
Pockets: 1 · best druggability 0.28

Structure

x-ray diffraction · 2 distinct chains · 7% helix, 53% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transthyretin	protein	114	6% helix, 54% strand	P02766
B	Transthyretin	protein	115	7% helix, 53% strand	P02766

Ligands and binding sites

HG6 · 4-chloranyl-9,10-bis(oxidanylidene)anthracene-2-carboxylic acid · ligand · 2 copies · chains A, B
CA · Calcium ion · metal · 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	63	0.28	0.74	14	empty

Interfaces

1 interface between chains.

A–B · 952 Å² buried · 18 hydrogen bonds · protein-protein

Compared structures

7DT3 · Crystal structure of human transthyretin in complex with… · 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 7DT3 · PDBe 7DT3 · UniProt P02766

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