MolNFT v1 · #8297 · protein

Human oestrogen receptor alpha ligand-binding domain in complex with raloxifene core and TIF2 NRBOX2 peptide

1GWQ: “Human oestrogen receptor alpha ligand-binding domain in complex with raloxifene core and TIF2 NRBOX2 peptide”. X-ray diffraction, 1 ligand (ZTW), 10 pockets (best druggability 0.83). MolNFT v1 #8297 on GenesisL1: 3D structure…

PDB: 1GWQ
Type: protein
Length: 503 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Oestrogen receptor; Nuclear receptor coactivator 2
UniProt: P03372, Q15596
Ligands: ZTW
Pockets: 10 · best druggability 0.83

Structure

x-ray diffraction · 3 distinct chains · 71% helix, 4% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Oestrogen receptor	protein	243	71% helix, 4% strand	P03372
B	Oestrogen receptor	protein	242	71% helix, 4% strand	P03372
C, D	Nuclear receptor coactivator 2	protein	9	78% helix, 0% strand	Q15596

Ligands and binding sites

ZTW · Raloxifene core · ligand · 2 copies · chains A, B

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

Pockets

10 pockets found on a 1 Å grid, 6 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	154	0.83	0.98	22	ZTW
2	147	0.82	0.97	21	ZTW
3	142	0.64	0.86	21	empty
4	150	0.63	0.85	26	empty
5	300	0.57	0.77	38	empty

Interfaces

3 interfaces between chains.

A–B · 1757 Å² buried · 24 hydrogen bonds · protein-protein
B–D · 480 Å² buried · 6 hydrogen bonds · protein-protein
A–C · 471 Å² buried · 8 hydrogen bonds · protein-protein

Compared structures

1GWQ · Human oestrogen receptor alpha ligand-binding domain in complex with raloxifene core and… · 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 0.97

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 Q15596
Elsewhere: RCSB PDB 1GWQ · PDBe 1GWQ · UniProt P03372 · UniProt Q15596

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