MolNFT v1 · #81554 · protein

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

3UUA · Estrogen receptor: “Crystal structure of hera-lbd (Y537S) in complex with bisphenol-af”. X-ray diffraction, 1 ligand (0CZ), 7 pockets (best druggability 0.85). MolNFT v1 #81554 on GenesisL1: 3D structure, binding sites and pockets…

PDB: 3UUA
Type: protein
Length: 490 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Estrogen receptor; Nuclear receptor coactivator 1
EC: 2.3.1.48
UniProt: P03372, Q15788
Ligands: 0CZ
Pockets: 7 · best druggability 0.85

Structure

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

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Estrogen receptor	protein	242	69% helix, 4% strand	P03372
B	Estrogen receptor	protein	230	73% helix, 4% strand	P03372
F, G	Nuclear receptor coactivator 1 (EC 2.3.1.48)	protein	9	78% helix, 0% strand	Q15788

Ligands and binding sites

0CZ · 4,4'-(1,1,1,3,3,3-hexafluoropropane-2,2-diyl)diphenol · ligand · 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	218	0.85	0.97	23	0CZ
2	246	0.84	0.96	26	0CZ
3	109	0.68	0.90	18	empty
4	109	0.65	0.89	19	empty
5	376	0.63	0.78	54	empty

Interfaces

3 interfaces between chains.

A–B · 1675 Å² buried · 25 hydrogen bonds · protein-protein
A–F · 504 Å² buried · 6 hydrogen bonds · protein-protein
B–G · 500 Å² buried · 3 hydrogen bonds · protein-protein

Modifications

Observed in the structure: 3 modified (oxidation).

Compared structures

3UUA · Crystal structure of hERa-LBD (Y537S) in complex with bisphenol-AF · 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 3UUA · PDBe 3UUA · UniProt P03372 · UniProt Q15788

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