Research workbench
Glucocorticoid receptor lbd bound to GSK866
Analyse Glucocorticoid receptor lbd bound to GSK866 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3E7C
- Type
- protein
- Length
- 514 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucocorticoid receptor; Nuclear receptor coactivator 2
- UniProt
- P04150, Q15596
- Ligands
- 866
- Pockets
- 4 · best druggability 0.85
Structure
x-ray diffraction · 4 distinct chains · 65% helix, 5% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucocorticoid receptor | protein | 248 | 65% helix, 5% strand | P04150 |
| H | Nuclear receptor coactivator 2 | protein | 11 | 64% helix, 0% strand | Q15596 |
| B | Glucocorticoid receptor | protein | 245 | 64% helix, 5% strand | P04150 |
| D | Nuclear receptor coactivator 2 | protein | 10 | 70% helix, 0% strand | Q15596 |
Ligands and binding sites
- 866 · 5-amino-N-[(2S)-2-({[(2,6-dichlorophenyl)carbonyl](ethyl)amino}methyl)-3,3,3-trifluoro-2-hydroxypropyl]-1-(4-fluorophenyl)-1H-pyrazole-4-carboxamide · ligand · 2 copies · chains A, B
- GOL · Glycerol · additive · 3 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 3 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 372 | 0.85 | 0.93 | 48 | 866, GOL |
| 2 | 353 | 0.85 | 0.93 | 46 | 866, GOL |
| 3 | 346 | 0.57 | 0.75 | 39 | empty |
| 4 | 125 | 0.39 | 0.75 | 20 | empty |
Interfaces
3 interfaces between chains.
- A–B · 694 Ų buried · 2 hydrogen bonds · protein-protein
- A–H · 604 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 580 Ų buried · 5 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 P04150
- Every structure of UniProt Q15596
- Elsewhere: RCSB PDB 3E7C · PDBe 3E7C · UniProt P04150 · UniProt Q15596
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