Research workbench
Crystal structure of the human mineralocorticoid receptor ligand- binding domain bound to progesterone and harboring the S810L mutation responsible for a severe form of hypertension
Analyse Crystal structure of the human mineralocorticoid receptor ligand- binding… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1YA3
- Type
- protein
- Length
- 695 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mineralocorticoid receptor
- UniProt
- P08235
- Ligands
- STR
- Pockets
- 10 · best druggability 0.84
Structure
x-ray diffraction · 3 distinct chains · 70% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mineralocorticoid receptor | protein | 233 | 69% helix, 6% strand | P08235 |
| B | Mineralocorticoid receptor | protein | 230 | 71% helix, 6% strand | P08235 |
| C | Mineralocorticoid receptor | protein | 232 | 70% helix, 6% strand | P08235 |
Ligands and binding sites
- STR · Progesterone · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
10 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 185 | 0.84 | 0.98 | 24 | STR |
| 2 | 197 | 0.83 | 0.96 | 24 | STR |
| 3 | 167 | 0.82 | 0.97 | 25 | STR |
| 4 | 194 | 0.66 | 0.85 | 24 | empty |
| 5 | 109 | 0.59 | 0.86 | 24 | empty |
Compared structures
- 1YA3 · Crystal structure of the human mineralocorticoid receptor ligand-binding domain bound to… · the same entry in another collection · chain A against A, TM-score 1.00
- P08235 · AlphaFold monomer V2.0 prediction for mineralocorticoid receptor (P08235) · a predicted model of the same protein · chain B against A, TM-score 0.99
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
- Elsewhere: RCSB PDB 1YA3 · PDBe 1YA3 · UniProt P08235
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.