MolNFT v1 · #107542 · protein
Gr in complex with dexamethasone
4UDC · Glucocorticoid receptor: “Gr in complex with dexamethasone”. X-ray diffraction, 2 ligands (CPS, DEX), 2 pockets (best druggability 0.84). MolNFT v1 #107542 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 4UDC
- Type
- protein
- Length
- 261 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucocorticoid receptor; Nuclear receptor coactivator 2
- UniProt
- P04150, Q15596
- Ligands
- CPS, DEX
- Pockets
- 2 · best druggability 0.84
Structure
x-ray diffraction · 2 distinct chains · 66% helix, 4% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glucocorticoid receptor | protein | 248 | 66% helix, 4% strand | P04150 |
| B | Nuclear receptor coactivator 2 | protein | 13 | 62% helix, 0% strand | Q15596 |
Ligands and binding sites
- CPS · 3-[(3-cholamidopropyl)dimethylammonio]-1-propanesulfonate · ligand · chains A
- DEX · Dexamethasone · ligand · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 204 | 0.84 | 0.97 | 25 | DEX |
| 2 | 143 | 0.65 | 0.87 | 19 | empty |
Interfaces
1 interface between chains.
- A–B · 665 Ų buried · 14 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 4UDC · PDBe 4UDC · UniProt P04150 · UniProt Q15596
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