Research workbench
Structural basis of heterodimeric ecdysteroid receptor interaction with natural response element HSP27 gene promoter
Analyse Structural basis of heterodimeric ecdysteroid receptor interaction with natural… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2HAN
- Type
- protein + DNA
- Length
- 205 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- 5'-D(*CP*AP*AP*GP*GP*GP*TP*TP*CP*AP*AP*TP*GP*CP*AP*CP*TP*TP *GP*T)-3'…
- UniProt
- P20153, P34021
- Ligands
- ZN
- Pockets
- 4 · best druggability 0.70
Structure
x-ray diffraction · 4 distinct chains · 38% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| C | 5'-D(*CP*AP*AP*GP*GP*GP*TP*TP*CP*AP*AP*TP*GP*CP*AP*CP*TP*TP *GP*T)-3' | dna | 20 | — | — |
| D | 5'-D(*GP*AP*CP*AP*AP*GP*TP*GP*CP*AP*TP*TP*GP*AP*AP*CP*CP*CP *TP*T)-3' | dna | 20 | — | — |
| A | Protein ultraspiracle | protein | 78 | 38% helix, 10% strand | P20153 |
| B | Ecdysone receptor | protein | 87 | 38% helix, 9% strand | P34021 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 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, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 675 | 0.70 | 0.78 | 64 | empty |
| 2 | 115 | 0.43 | 0.77 | 16 | empty |
| 3 | 142 | 0.38 | 0.74 | 24 | empty |
| 4 | 106 | 0.38 | 0.75 | 15 | empty |
Interfaces
6 interfaces between chains.
- C–D · 853 Ų buried · 78 hydrogen bonds · nucleic-nucleic
- C–B · 532 Ų buried · 11 hydrogen bonds · protein-nucleic
- D–B · 506 Ų buried · 12 hydrogen bonds · protein-nucleic
- C–A · 489 Ų buried · 11 hydrogen bonds · protein-nucleic
- D–A · 417 Ų buried · 12 hydrogen bonds · protein-nucleic
Compared structures
- 2HAN · Structural basis of heterodimeric ecdysteroid receptor interaction with natural response… · the same entry in another collection · chain C against C, TM-score 1.00
- P20153 · AlphaFold monomer V2.0 prediction for protein ultraspiracle (P20153) · a predicted model of the same protein · chain A against A, TM-score 0.98
- P34021 · AlphaFold monomer V2.0 prediction for ecdysone receptor (P34021) · a predicted model of the same protein · chain B against A, TM-score 0.90
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 P20153
- Every structure of UniProt P34021
- Elsewhere: RCSB PDB 2HAN · PDBe 2HAN · UniProt P20153 · UniProt P34021
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.