Research workbench
Isotype selectivity of the human retinoic acid nuclear receptor hrar: the complex with the RARBETA/GAMMA-selective retinoid CD564
Analyse Isotype selectivity of the human retinoic acid nuclear receptor hrar: the… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1FCY
- Type
- protein
- Length
- 236 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Retinoic acid receptor gamma-1
- UniProt
- P13631
- Ligands
- 564, LMU
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 69% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retinoic acid receptor gamma-1 | protein | 236 | 69% helix, 4% strand | P13631 |
Ligands and binding sites
- 564 · 6-(5,5,8,8-tetramethyl-5,6,7,8-tetrahydro-naphtalene-2-carbonyl)-naphtalene-2-carboxylic acid · ligand · chains A
- LMU · Dodecyl-alpha-D-maltoside · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 222 | 0.81 | 0.94 | 35 | 564 |
| 2 | 108 | 0.49 | 0.81 | 19 | empty |
| 3 | 69 | 0.40 | 0.79 | 12 | empty |
| 4 | 99 | 0.36 | 0.74 | 16 | empty |
Compared structures
- 1FCY · Isotype selectivity of the human retinoic acid nuclear receptor hrar: the complex with… · the same entry in another collection · chain A against A, TM-score 1.00
- P13631 · AlphaFold monomer V2.0 prediction for retinoic acid receptor gamma (P13631) · 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 P13631
- Elsewhere: RCSB PDB 1FCY · PDBe 1FCY · UniProt P13631
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