MolNFT v1 · #92233 · protein
Structural basis for the accommodation of bis- and tris-aromatic derivatives in vitamin D nuclear receptor
4G1D: “Structural basis for the accommodation of bis- and tris-aromatic derivatives in vitamin D nuclear receptor”. X-ray diffraction. MolNFT v1 #92233 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4G1D
- Type
- protein
- Length
- 250 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9PTN2, Q15788
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 239 | — | Q9PTN2 |
| B | — | protein | 11 | — | Q15788 |
Compared structures
- 4G1D · Structural basis for the accommodation of bis- and tris-aromatic derivatives in Vitamin D… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9PTN2 · AlphaFold monomer V2.0 prediction for vitamin D3 receptor a (Q9PTN2) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q15788
- Elsewhere: RCSB PDB 4G1D · PDBe 4G1D · UniProt Q9PTN2 · UniProt Q15788
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