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Crystal structure of V30M mutated transthyretin in complex with 3- isomangostin

Analyse Crystal structure of V30M mutated transthyretin in complex with 3- isomangostin in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 4Y9G
Type: protein
Length: 231 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Ligands: MKU
Pockets: 1 · best druggability 0.34

Structure

x-ray diffraction · 2 distinct chains · 6% helix, 51% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transthyretin	protein	116	6% helix, 51% strand	P02766
B	Transthyretin	protein	115	7% helix, 51% strand	P02766

Ligands and binding sites

MKU · 5,9-dihydroxy-8-methoxy-2,2-dimethyl-7-(3-methylbut-2-en-1-yl)-3,4-dihydro-2H,6H-pyrano[3,2-b]xanthen-6-one · 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	68	0.34	0.76	16	empty

Interfaces

1 interface between chains.

A–B · 920 Å² buried · 20 hydrogen bonds · protein-protein

Compared structures

4Y9G · Crystal structure of V30M mutated transthyretin in complex with 3-isomangostin · 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 4Y9G · PDBe 4Y9G · UniProt P02766

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