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Crystal structure of the hpxr-lbd in complex with ferutinine

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

PDB: 7AXC
Type: protein
Length: 264 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Nuclear receptor subfamily 1 group I member 2
UniProt: O75469
Ligands: 27H
Pockets: 2 · best druggability 0.81

Structure

x-ray diffraction · 1 distinct chain · 61% helix, 8% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Nuclear receptor subfamily 1 group I member 2	protein	264	61% helix, 8% strand	O75469

Ligands and binding sites

27H · ferutinine · ligand · chains A
IPA · Isopropyl alcohol · additive · 4 copies · chains A
GOL · Glycerol · additive · 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, 1 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	762	0.81	0.84	70	27H
2	53	0.31	0.77	12	empty

Compared structures

7AXC · Crystal structure of the hPXR-LBD in complex with ferutinine · the same entry in another collection · chain A against A, TM-score 1.00
O75469 · AlphaFold monomer V2.0 prediction for nuclear receptor subfamily 1 group I member 2… · 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 O75469
Elsewhere: RCSB PDB 7AXC · PDBe 7AXC · UniProt O75469

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