MolNFT v1 · #152058 · protein

Crystal structure of human errg lbd in complex with 4-sec-butylphenol

6I66 · Estrogen-related receptor gamma: “Crystal structure of human errg lbd in complex with 4-sec-butylphenol”. X-ray diffraction, 1 ligand (H4Q), 3 pockets (best druggability 0.77). MolNFT v1 #152058 on GenesisL1: 3D structure, binding…

PDB: 6I66
Type: protein
Length: 223 residues
Chains: 1
Method: x-ray diffraction
Collection: MolNFT v1 / PDB
Contract: 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
Owner: 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
Molecule: Estrogen-related receptor gamma
UniProt: P62508
Ligands: H4Q
Pockets: 3 · best druggability 0.77

Structure

x-ray diffraction · 1 distinct chain · 67% helix, 3% strand (DSSP).

Chain	Molecule	Type	Residues	Secondary structure	UniProt
A	Estrogen-related receptor gamma	protein	223	67% helix, 3% strand	P62508

Ligands and binding sites

H4Q · 4-[(2~{R})-butan-2-yl]phenol · ligand · chains A
GOL · Glycerol · additive · 2 copies · chains A

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

Pockets

3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.

Pocket	Volume (Å³)	Druggability	Buriedness	Lining residues	Inside
1	82	0.77	0.98	18	H4Q
2	144	0.62	0.85	23	GOL
3	78	0.33	0.75	19	empty

Compared structures

6I66 · Crystal structure of human ERRg LBD in complex with 4-sec-butylphenol · the same entry in another collection · chain A against A, TM-score 1.00
P62508 · AlphaFold monomer V2.0 prediction for estrogen-related receptor gamma (P62508) · a predicted model of the same protein · chain A 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 P62508
Elsewhere: RCSB PDB 6I66 · PDBe 6I66 · UniProt P62508

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