MolNFT v1 · #64551 · protein + DNA
Gr DNA binding DOMAIN:FKBP5 binding site complex-9
3G6Q · Glucocorticoid receptor: “Gr DNA binding DOMAIN:FKBP5 binding site complex-9”. X-ray diffraction, 1 ligand (ZN), 5 pockets (best druggability 0.69). MolNFT v1 #64551 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 3G6Q
- Type
- protein + DNA
- Length
- 184 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glucocorticoid receptor; DNA (5'-D(*TP*AP*GP*AP*AP*CP*AP*GP*GP*GP*TP*GP*TP*TP*CP*T)- 3')…
- UniProt
- P06536
- Ligands
- ZN
- Pockets
- 5 · best druggability 0.69
Structure
x-ray diffraction · 4 distinct chains · 32% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | Glucocorticoid receptor | protein | 74 | 30% helix, 11% strand | P06536 |
| A | Glucocorticoid receptor | protein | 78 | 33% helix, 8% strand | P06536 |
| C | DNA (5'-D(*TP*AP*GP*AP*AP*CP*AP*GP*GP*GP*TP*GP*TP*TP*CP*T)- 3') | dna | 16 | — | — |
| D | DNA (5'-D(*AP*AP*GP*AP*AP*CP*AP*CP*CP*CP*TP*GP*TP*TP*CP*T)- 3') | dna | 16 | — | — |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains B, A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
5 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 518 | 0.69 | 0.80 | 37 | empty |
| 2 | 83 | 0.39 | 0.78 | 17 | empty |
| 3 | 92 | 0.38 | 0.77 | 20 | empty |
| 4 | 60 | 0.32 | 0.76 | 14 | empty |
| 5 | 59 | 0.27 | 0.74 | 14 | empty |
Interfaces
6 interfaces between chains.
- C–D · 644 Ų buried · 66 hydrogen bonds · nucleic-nucleic
- B–A · 554 Ų buried · 10 hydrogen bonds · protein-protein
- B–C · 417 Ų buried · 9 hydrogen bonds · protein-nucleic
- B–D · 356 Ų buried · 6 hydrogen bonds · protein-nucleic
- A–C · 348 Ų buried · 6 hydrogen bonds · protein-nucleic
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 P06536
- Elsewhere: RCSB PDB 3G6Q · PDBe 3G6Q · UniProt P06536
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.