MolNFT v1 · #74287 · protein

Estrogen receptor

3OSA: “Estrogen receptor”. X-ray diffraction, 1 ligand (KN3), 18 pockets (best druggability 0.84). MolNFT v1 #74287 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 3OSA
Type: protein
Length: 934 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Estrogen receptor
UniProt: P03372
Ligands: KN3
Pockets: 18 · best druggability 0.84

Structure

x-ray diffraction · 4 distinct chains · 69% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Estrogen receptor	protein	239	67% helix, 4% strand	P03372
B	Estrogen receptor	protein	239	67% helix, 4% strand	P03372
C	Estrogen receptor	protein	230	72% helix, 4% strand	P03372
D	Estrogen receptor	protein	226	72% helix, 4% strand	P03372

Ligands and binding sites

KN3 · 4-[1-(3-methylbut-2-en-1-yl)-7-(trifluoromethyl)-1H-indazol-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

18 pockets found on a 1 Å grid, 13 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	216	0.84	0.96	24	KN3
2	219	0.83	0.95	27	KN3
3	287	0.82	0.92	38	KN3
4	279	0.81	0.92	35	KN3
5	421	0.66	0.79	51	empty

Interfaces

5 interfaces between chains.

B–D · 1636 Å² buried · 28 hydrogen bonds · protein-protein
A–C · 1557 Å² buried · 29 hydrogen bonds · protein-protein
A–B · 246 Å² buried · 3 hydrogen bonds · protein-protein
B–C · 64 Å² buried · 0 hydrogen bonds · protein-protein
A–D · 60 Å² buried · 0 hydrogen bonds · protein-protein

Compared structures

3OSA · Estrogen Receptor · the same entry in another collection · chain D against D, TM-score 1.00
P03372 · AlphaFold monomer V2.0 prediction for estrogen receptor (P03372) · a predicted model of the same protein · chain D 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 P03372
Elsewhere: RCSB PDB 3OSA · PDBe 3OSA · UniProt P03372

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