Research workbench

Nischarin px-domain

Analyse Nischarin px-domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 3P0C
Type: protein
Length: 219 residues
Chains: 2
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nischarin
UniProt: Q9Y2I1
Pockets: 2 · best druggability 0.28

Structure

x-ray diffraction · 2 distinct chains · 37% helix, 23% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nischarin	protein	111	34% helix, 23% strand	Q9Y2I1
B	Nischarin	protein	108	39% helix, 22% strand	Q9Y2I1

Ligands and binding sites

GOL · Glycerol · additive · 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	58	0.28	0.74	21	empty
2	53	0.28	0.74	12	empty

Interfaces

1 interface between chains.

A–B · 586 Å² buried · 15 hydrogen bonds · protein-protein

Compared structures

3P0C · Nischarin PX-domain · the same entry in another collection · chain A against A, TM-score 1.00
Q9Y2I1 · AlphaFold monomer V2.0 prediction for nischarin (Q9Y2I1) · a predicted model of the same protein · chain B against A, TM-score 0.83

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 Q9Y2I1
Elsewhere: RCSB PDB 3P0C · PDBe 3P0C · UniProt Q9Y2I1

GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.