Research workbench
Vitamin D nuclear receptor complex 4
Analyse Vitamin D nuclear receptor complex 4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FO8
- Type
- protein
- Length
- 245 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vitamin D3 receptor a; Nuclear receptor coactivator 1
- UniProt
- Q9PTN2
- Ligands
- DZT
- Pockets
- 2 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 66% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| 1 | Vitamin D3 receptor a | protein | 236 | 66% helix, 3% strand | Q9PTN2 |
| B | Nuclear receptor coactivator 1 | protein | 9 | 67% helix, 0% strand | — |
Ligands and binding sites
- DZT · (1~{R},3~{S},5~{Z})-4-methylidene-5-[(~{E})-3-[3-(6-methyl-6-oxidanyl-heptyl)phenyl]non-2-enylidene]cyclohexane-1,3-diol · ligand · chains 1
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 | 308 | 0.86 | 0.96 | 40 | DZT |
| 2 | 136 | 0.41 | 0.75 | 26 | empty |
Interfaces
1 interface between chains.
- 1–B · 550 Ų buried · 7 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
- Elsewhere: RCSB PDB 6FO8 · PDBe 6FO8 · UniProt Q9PTN2
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