Research workbench
Diastereotopic and deuterium effects in gemini
Analyse Diastereotopic and deuterium effects in gemini in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4IA2
- Type
- protein
- Length
- 249 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vitamin D3 receptor a; Nuclear receptor coactivator 2
- UniProt
- Q9PTN2, Q15596
- Ligands
- BIV
- Pockets
- 2 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 67% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vitamin D3 receptor a | protein | 239 | 68% helix, 2% strand | Q9PTN2 |
| B | Nuclear receptor coactivator 2 | protein | 10 | 60% helix, 0% strand | Q15596 |
Ligands and binding sites
- BIV · 21-nor-9,10-secocholesta-5,7,10(19)-triene-1,3,25-triol, 20-(4-hydroxy-4-methylpentyl)-, (1A,3B,5Z,7E) · 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 387 | 0.86 | 0.94 | 42 | BIV |
| 2 | 183 | 0.48 | 0.76 | 29 | empty |
Interfaces
1 interface between chains.
- A–B · 567 Ų buried · 6 hydrogen bonds · protein-protein
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 Q9PTN2
- Every structure of UniProt Q15596
- Elsewhere: RCSB PDB 4IA2 · PDBe 4IA2 · UniProt Q9PTN2 · UniProt Q15596
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