MolNFT v1 · #99857 · protein

Crystal structure of hera-lbd (Y537S) in complex with butylparaben

4MG9 · Estrogen receptor: “Crystal structure of hera-lbd (Y537S) in complex with butylparaben”. X-ray diffraction, 1 ligand (27K), 7 pockets (best druggability 0.84). MolNFT v1 #99857 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 4MG9
Type: protein
Length: 493 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Estrogen receptor; Nuclear receptor coactivator 1
UniProt: P03372, Q15788
Ligands: 27K
Pockets: 7 · best druggability 0.84

Structure

x-ray diffraction · 3 distinct chains · 70% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Estrogen receptor	protein	242	70% helix, 3% strand	P03372
B	Estrogen receptor	protein	233	70% helix, 4% strand	P03372
F, G	Nuclear receptor coactivator 1	protein	9	78% helix, 0% strand	Q15788

Ligands and binding sites

27K · butyl 4-hydroxybenzoate · ligand · 2 copies · chains A, B
GOL · Glycerol · additive · 2 copies · chains A, B

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

Pockets

7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	170	0.84	0.98	21	27K
2	267	0.81	0.92	40	27K
3	83	0.62	0.89	17	empty
4	81	0.62	0.90	18	empty
5	201	0.52	0.77	27	empty

Interfaces

3 interfaces between chains.

A–B · 1678 Å² buried · 24 hydrogen bonds · protein-protein
A–F · 520 Å² buried · 3 hydrogen bonds · protein-protein
B–G · 484 Å² buried · 4 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 4 modified (oxidation).

Compared structures

4MG9 · Crystal structure of hERa-LBD (Y537S) in complex with butylparaben · 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 B against A, TM-score 0.99

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
Every structure of UniProt Q15788
Elsewhere: RCSB PDB 4MG9 · PDBe 4MG9 · UniProt P03372 · UniProt Q15788

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