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Structure of mouse asterc (GRAMD1C) with a new cholesterol-derived compound

Analyse Structure of mouse asterc (GRAMD1C) with a new cholesterol-derived compound in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 7AZN
Type: protein
Length: 177 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Protein aster-C
UniProt: Q8CI52
Ligands: YK8
Pockets: 1 · best druggability 0.79

Structure

x-ray diffraction · 1 distinct chain · 32% helix, 39% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Protein aster-C	protein	177	32% helix, 39% strand	Q8CI52

Ligands and binding sites

YK8 · 20alpha-hydroxy-20-(5-methylhexyl)cholesterol · ligand · chains A
EOH · Ethanol · additive · 6 copies · chains A
GOL · Glycerol · additive · chains A

Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.

Pockets

1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	469	0.79	0.86	49	YK8, EOH, GOL

Compared structures

7AZN · Structure of mouse AsterC (GramD1c) with a new cholesterol-derived compound · the same entry in another collection · chain A against A, TM-score 1.00
Q8CI52 · AlphaFold monomer V2.0 prediction for protein aster-C (Q8CI52) · a predicted model of the same protein · chain A against A, TM-score 0.98

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 Q8CI52
Elsewhere: RCSB PDB 7AZN · PDBe 7AZN · UniProt Q8CI52

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