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Crystal structure of human transthyretin in complex with 2,6-dinitro- P-cresol (dnpc)

Analyse Crystal structure of human transthyretin in complex with 2,6-dinitro- P-cresol… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 5L4F
Type: protein
Length: 231 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Ligands: 6J1, NA
Pockets: 2 · best druggability 0.32

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Transthyretin	protein	116	6% helix, 53% strand	P02766
B	Transthyretin	protein	115	6% helix, 53% strand	P02766

Ligands and binding sites

6J1 · 2,6-Dinitro-p-cresol · ligand · 2 copies · chains A, B
NA · Sodium ion · metal · 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	74	0.32	0.75	15	empty
2	50	0.31	0.77	13	empty

Interfaces

1 interface between chains.

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

Compared structures

5L4F · Crystal Structure of Human Transthyretin in Complex with 2,6-Dinitro-p-cresol (DNPC) · the same entry in another collection · chain A against A, TM-score 1.00

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Every structure of UniProt P02766
Elsewhere: RCSB PDB 5L4F · PDBe 5L4F · UniProt P02766

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