MolNFT v1 · #37986 · protein

Human estrogen receptor beta ligand-binding domain in complex with compound 45

2GIU: “Human estrogen receptor beta ligand-binding domain in complex with compound 45”. X-ray diffraction, 1 ligand (FBR), 2 pockets (best druggability 0.83). MolNFT v1 #37986 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 2GIU
Type: protein
Length: 225 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Estrogen receptor beta
UniProt: Q92731
Ligands: FBR
Pockets: 2 · best druggability 0.83

Structure

x-ray diffraction · 1 distinct chain · 71% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Estrogen receptor beta	protein	225	71% helix, 4% strand	Q92731

Ligands and binding sites

FBR · (9aS)-4-bromo-9a-butyl-7-hydroxy-1,2,9,9a-tetrahydro-3H-fluoren-3-one · 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	194	0.83	0.96	24	FBR
2	99	0.55	0.84	20	empty

Compared structures

2GIU · Human estrogen receptor beta ligand-binding domain in complex with compound 45 · the same entry in another collection · chain A against A, TM-score 1.00
Q92731 · AlphaFold monomer V2.0 prediction for estrogen receptor beta (Q92731) · a predicted model of the same protein · chain A against A, TM-score 0.92

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 Q92731
Elsewhere: RCSB PDB 2GIU · PDBe 2GIU · UniProt Q92731

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