MolNFT v2 · #116953 · protein

Crystal Structure of the ER-alpha Ligand-binding Domain in complex with a t-butyl-substituted, methyl, triaryl-ethylene derivative 4,4'-[2-(4-tert-butylphenyl)prop-1-ene-1,1-diyl]diphenol

5DKG: “Crystal Structure of the ER-alpha Ligand-binding Domain in complex with a t-butyl-substituted, methyl…”. X-ray diffraction at 2.15, 1 ligand (5C7). MolNFT v2 #116953 on GenesisL1: 3D structure, binding sites and pockets in GL1X.

PDB: 5DKG
Type: protein
Length: 491 residues
Chains: 4
Method: x-ray diffraction
Collection: MolNFT v2 / PDB Bank
Contract: 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
Owner: 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
Resolution: 2.15
Source: Homo sapiens; SYNTHETIC CONSTRUCT
UniProt: P03372, Q15596
Ligands: 5C7

Structure

x-ray diffraction · resolution 2.15 · 3 distinct chains.

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	—	protein	231	—	P03372
B	—	protein	240	—	P03372
C, D	—	protein	10	—	Q15596

Ligands and binding sites

5C7 · 4,4'-[2-(4-tert-butylphenyl)prop-1-ene-1,1-diyl]diphenol · ligand · 2 copies · chains A, B

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

Compared structures

5DKG · Crystal structure of the er-alpha ligand-binding domain in complex with a… · 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 A 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 P03372
Every structure of UniProt Q15596
Elsewhere: RCSB PDB 5DKG · PDBe 5DKG · UniProt P03372 · UniProt Q15596

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