MolNFT v1 · #38185 · protein
Estrogen related receptor-gamma ligand binding domain complexed with a synthetic peptide from RIP140
2GPO · Estrogen-related receptor gamma: “Estrogen related receptor-gamma ligand binding domain complexed with a synthetic peptide from RIP140”. X-ray diffraction, 2 pockets (best druggability 0.77). MolNFT v1 #38185 on GenesisL1: 3D…
- PDB
- 2GPO
- Type
- protein
- Length
- 234 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Estrogen-related receptor gamma; Nuclear receptor-interacting protein 1
- UniProt
- P62508, P48552
- Pockets
- 2 · best druggability 0.77
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Estrogen-related receptor gamma | protein | 224 | 69% helix, 3% strand | P62508 |
| C | Nuclear receptor-interacting protein 1 | protein | 10 | 70% helix, 0% strand | P48552 |
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 | 79 | 0.77 | 0.98 | 16 | empty |
| 2 | 124 | 0.67 | 0.89 | 22 | empty |
Interfaces
1 interface between chains.
- A–C · 485 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2GPO · Estrogen Related Receptor-gamma ligand binding domain complexed with a synthetic peptide… · 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
- P48552 · AlphaFold monomer V2.0 prediction for nuclear receptor-interacting protein 1 (P48552) · a predicted model of the same protein · chain C against A, TM-score 0.78
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
- Every structure of UniProt P48552
- Elsewhere: RCSB PDB 2GPO · PDBe 2GPO · UniProt P62508 · UniProt P48552
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