Research workbench
Mineralocorticoid receptor S810L mutant with bound progesterone
Analyse Mineralocorticoid receptor S810L mutant with bound progesterone in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2AA6
- Type
- protein
- Length
- 519 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mineralocorticoid receptor
- UniProt
- P08235
- Ligands
- STR
- Pockets
- 8 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 67% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mineralocorticoid receptor | protein | 260 | 67% helix, 5% strand | P08235 |
| B | Mineralocorticoid receptor | protein | 259 | 68% helix, 5% strand | P08235 |
Ligands and binding sites
- STR · Progesterone · ligand · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
8 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 173 | 0.84 | 0.98 | 23 | STR |
| 2 | 175 | 0.83 | 0.97 | 23 | STR |
| 3 | 122 | 0.68 | 0.90 | 20 | empty |
| 4 | 139 | 0.65 | 0.87 | 19 | empty |
| 5 | 79 | 0.46 | 0.81 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 727 Ų buried · 11 hydrogen bonds · protein-protein
Compared structures
- 2AA6 · Mineralocorticoid Receptor S810L Mutant with Bound Progesterone · 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 0.97
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 P08235
- Elsewhere: RCSB PDB 2AA6 · PDBe 2AA6 · UniProt P08235
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