Research workbench
Crystal structure of the resurrected ancestral glucocorticoid receptor 1 in complex with doc
Analyse Crystal structure of the resurrected ancestral glucocorticoid receptor 1 in… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3RY9
- Type
- protein
- Length
- 490 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ancestral glucocorticoid receptor 1
- Ligands
- 1CA, NA
- Pockets
- 7 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 69% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ancestral glucocorticoid receptor 1 | protein | 243 | 68% helix, 5% strand | — |
| B | Ancestral glucocorticoid receptor 1 | protein | 247 | 69% helix, 5% strand | — |
Ligands and binding sites
- 1CA · Desoxycorticosterone · ligand · 2 copies · chains A, B
- NA · Sodium ion · metal · chains B
- GOL · Glycerol · additive · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
7 pockets found on a 1 Å grid, 5 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 178 | 0.84 | 0.98 | 24 | 1CA |
| 2 | 178 | 0.84 | 0.97 | 23 | 1CA |
| 3 | 152 | 0.70 | 0.89 | 24 | empty |
| 4 | 157 | 0.67 | 0.87 | 21 | empty |
| 5 | 354 | 0.63 | 0.79 | 44 | GOL |
Interfaces
1 interface between chains.
- A–B · 671 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 3RY9 · Crystal Structure of the Resurrected Ancestral Glucocorticoid Receptor 1 in complex with… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Elsewhere: RCSB PDB 3RY9 · PDBe 3RY9
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