Research workbench
Ligand-binding domain of the human retinoic acid receptor gamma bound to all-trans retinoic acid
Analyse Ligand-binding domain of the human retinoic acid receptor gamma bound to… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2LBD
- Type
- protein
- Length
- 238 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Retinoic acid receptor gamma
- UniProt
- P22932
- Ligands
- REA
- Pockets
- 4 · best druggability 0.81
Structure
x-ray diffraction · 1 distinct chain · 68% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Retinoic acid receptor gamma | protein | 238 | 68% helix, 4% strand | P22932 |
Ligands and binding sites
- REA · Retinoic acid · 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 | 214 | 0.81 | 0.94 | 35 | REA |
| 2 | 115 | 0.47 | 0.79 | 18 | empty |
| 3 | 82 | 0.40 | 0.77 | 15 | empty |
| 4 | 56 | 0.33 | 0.77 | 16 | empty |
Compared structures
- 2LBD · Ligand-binding domain of the human retinoic acid receptor gamma bound to all-trans… · the same entry in another collection · chain A against A, TM-score 1.00
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 P22932
- Elsewhere: RCSB PDB 2LBD · PDBe 2LBD · UniProt P22932
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