Research workbench
Crystal structure of the human mineralocorticoid receptor ligand- binding domain bound to deoxycorticosterone
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
- 2ABI
- Type
- protein
- Length
- 698 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Mineralocorticoid receptor
- UniProt
- P08235
- Ligands
- 1CA
- Pockets
- 9 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 6% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Mineralocorticoid receptor | protein | 230 | 70% helix, 6% strand | P08235 |
| B, C | Mineralocorticoid receptor | protein | 234 | 68% helix, 6% strand | P08235 |
Ligands and binding sites
- 1CA · Desoxycorticosterone · ligand · 3 copies · chains A, B, C
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 8 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 183 | 0.83 | 0.97 | 23 | 1CA |
| 2 | 173 | 0.83 | 0.97 | 24 | 1CA |
| 3 | 167 | 0.83 | 0.97 | 23 | 1CA |
| 4 | 169 | 0.70 | 0.88 | 23 | empty |
| 5 | 117 | 0.65 | 0.88 | 22 | empty |
Compared structures
- 2ABI · 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 2ABI · PDBe 2ABI · UniProt P08235
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