MolNFT v1 · #152054 · protein
Crystal structure of human errg lbd in complex with hpte
6I62 · Estrogen-related receptor gamma: “Crystal structure of human errg lbd in complex with hpte”. X-ray diffraction, 1 ligand (27N), 2 pockets (best druggability 0.81). MolNFT v1 #152054 on GenesisL1: 3D structure, binding sites and…
- PDB
- 6I62
- Type
- protein
- Length
- 224 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen-related receptor gamma
- UniProt
- P62508
- Ligands
- 27N
- Pockets
- 2 · best druggability 0.81
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 | 224 | 67% helix, 3% strand | P62508 |
Ligands and binding sites
- 27N · 4,4'-(2,2,2-trichloroethane-1,1-diyl)diphenol · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 122 | 0.81 | 0.98 | 21 | 27N |
| 2 | 151 | 0.62 | 0.85 | 23 | empty |
Compared structures
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 6I62 · PDBe 6I62 · UniProt P62508
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