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Crystal structure of estrogen receptor beta complexed with cl-272

Analyse Crystal structure of estrogen receptor beta complexed with cl-272 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.

PDB: 1U3Q
Type: protein
Length: 905 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Estrogen receptor beta
UniProt: Q92731
Ligands: 272
Pockets: 15 · best druggability 0.83

Structure

x-ray diffraction · 2 distinct chains · 70% helix, 5% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A, C, D	Estrogen receptor beta	protein	226	71% helix, 5% strand	Q92731
B	Estrogen receptor beta	protein	227	70% helix, 5% strand	Q92731

Ligands and binding sites

272 · 4-(6-hydroxy-benzo[d]isoxazol-3-yl)benzene-1,3-diol · ligand · 4 copies · chains A, B, C, D

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

Pockets

15 pockets found on a 1 Å grid, 12 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	147	0.83	0.99	23	272
2	146	0.82	0.98	21	272
3	151	0.82	0.97	21	272
4	142	0.82	0.97	21	272
5	722	0.78	0.83	69	empty

Interfaces

5 interfaces between chains.

A–C · 1476 Å² buried · 16 hydrogen bonds · protein-protein
B–D · 1412 Å² buried · 11 hydrogen bonds · protein-protein
A–B · 597 Å² buried · 1 hydrogen bond · protein-protein
A–D · 240 Å² buried · 1 hydrogen bond · protein-protein
B–C · 185 Å² buried · 5 hydrogen bonds · protein-protein

Compared structures

1U3Q · Crystal Structure of Estrogen Receptor beta complexed with CL-272 · the same entry in another collection · chain D against D, TM-score 1.00
Q92731 · AlphaFold monomer V2.0 prediction for estrogen receptor beta (Q92731) · a predicted model of the same protein · chain C 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 Q92731
Elsewhere: RCSB PDB 1U3Q · PDBe 1U3Q · UniProt Q92731

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