MolNFT v1 · #31629 · protein

The crystal structure of 2,4-dinitrophenol in complex with human transthyretin

2B15: “The crystal structure of 2,4-dinitrophenol in complex with human transthyretin”. X-ray diffraction, 2 ligands (DNF, SO4), 2 pockets (best druggability 0.30). MolNFT v1 #31629 on GenesisL1: 3D structure, binding sites and pockets in…

PDB: 2B15
Type: protein
Length: 231 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Transthyretin
UniProt: P02766
Ligands: DNF, SO4
Pockets: 2 · best druggability 0.30

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, 48% strand	P02766
B	Transthyretin	protein	115	6% helix, 53% strand	P02766

Ligands and binding sites

DNF · 2,4-dinitrophenol · ligand · 2 copies · chains A, B
SO4 · Sulfate ion · ion · 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	68	0.30	0.74	16	empty
2	60	0.29	0.73	14	SO4

Interfaces

1 interface between chains.

A–B · 922 Å² buried · 17 hydrogen bonds · protein-protein

Compared structures

2B15 · The crystal structure of 2,4-dinitrophenol in complex with human transthyretin · 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 2B15 · PDBe 2B15 · UniProt P02766

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