Research workbench
Vitamin D3 RECEPTOR/LITHOCHORIC acid derivative complex
Analyse Vitamin D3 RECEPTOR/LITHOCHORIC acid derivative complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7C7V
- Type
- protein
- Length
- 247 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Vitamin D3 receptor; Mediator of RNA polymerase II transcription subunit 1
- UniProt
- P13053, Q15648
- Ligands
- FKC
- Pockets
- 2 · best druggability 0.86
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 3% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Vitamin D3 receptor | protein | 237 | 68% helix, 3% strand | P13053 |
| C | Mediator of RNA polymerase II transcription subunit 1 | protein | 10 | 70% helix, 0% strand | Q15648 |
Ligands and binding sites
- FKC · (4R)-4-[(3R,5R,8R,9S,10S,13R,14S,17R)-10,13-dimethyl-3-(2-methyl-2-oxidanyl-propyl)-2,3,4,5,6,7,8,9,11,12,14, 15,16,17-tetradecahydro-1H-cyclopenta[a]phenanthren-17-yl]pentanoic acid · ligand · chains A
- FMT · Formic acid · additive · 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 | 363 | 0.86 | 0.95 | 39 | FKC |
| 2 | 80 | 0.35 | 0.76 | 18 | empty |
Interfaces
1 interface between chains.
- A–C · 554 Ų buried · 9 hydrogen bonds · protein-protein
Compared structures
- 7C7V · Vitamin D3 receptor/lithochoric acid derivative complex · the same entry in another collection · chain A against A, TM-score 1.00
- Q15648 · AlphaFold monomer V2.0 prediction for mediator of RNA polymerase II transcription subunit… · a predicted model of the same protein · chain C against A, TM-score 0.80
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 P13053
- Every structure of UniProt Q15648
- Elsewhere: RCSB PDB 7C7V · PDBe 7C7V · UniProt P13053 · UniProt Q15648
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