Research workbench
Ancestral corticiod receptor in complex with doc
Analyse Ancestral corticiod receptor in complex with doc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2Q3Y
- Type
- protein
- Length
- 254 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ancestral corticiod receptor; Nuclear receptor 0B2
- UniProt
- Q15466
- Ligands
- 1CA
- Pockets
- 3 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 68% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ancestral corticiod receptor | protein | 244 | 68% helix, 5% strand | — |
| B | Nuclear receptor 0B2 | protein | 10 | 70% helix, 0% strand | Q15466 |
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 | 177 | 0.84 | 0.98 | 23 | 1CA |
| 2 | 137 | 0.64 | 0.86 | 21 | empty |
| 3 | 110 | 0.47 | 0.79 | 23 | empty |
Interfaces
1 interface between chains.
- A–B · 603 Ų buried · 4 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 Q15466
- Elsewhere: RCSB PDB 2Q3Y · PDBe 2Q3Y · UniProt Q15466
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