Research workbench
Mr in complex with dexamethasone
Analyse Mr in complex with dexamethasone in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UDA
- Type
- protein
- Length
- 252 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mineralocorticoid receptor; Nuclear receptor coactivator 1
- EC
- 2.3.1.48
- UniProt
- P08235, Q15788
- Ligands
- DEX
- Pockets
- 3 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mineralocorticoid receptor | protein | 242 | 69% helix, 5% strand | P08235 |
| B | Nuclear receptor coactivator 1 (EC 2.3.1.48) | protein | 10 | 60% helix, 0% strand | Q15788 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 186 | 0.84 | 0.98 | 23 | DEX |
| 2 | 109 | 0.64 | 0.88 | 21 | empty |
| 3 | 99 | 0.47 | 0.80 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 537 Ų buried · 2 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 P08235
- Every structure of UniProt Q15788
- Elsewhere: RCSB PDB 4UDA · PDBe 4UDA · UniProt P08235 · UniProt Q15788
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