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Human estrogen receptor alpha ligand-binding domain in complex with compound 11F

Analyse Human estrogen receptor alpha ligand-binding domain in complex with compound 11F in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 2IOG
Type: protein
Length: 243 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Estrogen receptor
UniProt: P03372
Ligands: IOG
Pockets: 2 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 67% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Estrogen receptor	protein	243	67% helix, 3% strand	P03372

Ligands and binding sites

IOG · N-[(1R)-3-(4-hydroxyphenyl)-1-methylpropyl]-2-[2-phenyl-6-(2-piperidin-1-ylethoxy)-1H-indol-3-yl]acetamide · ligand · 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, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	367	0.83	0.92	38	IOG
2	107	0.62	0.87	22	empty

Compared structures

2IOG · Human estrogen receptor alpha ligand-binding domain in complex with compound 11F · the same entry in another collection · chain A against A, TM-score 1.00
P03372 · AlphaFold monomer V2.0 prediction for estrogen receptor (P03372) · a predicted model of the same protein · chain A against A, TM-score 0.89

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 P03372
Elsewhere: RCSB PDB 2IOG · PDBe 2IOG · UniProt P03372

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