Research workbench
Crystal structure of the ets domain of human ETV5 in complex with DNA
Analyse Crystal structure of the ets domain of human ETV5 in complex with DNA in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4UNO
- Type
- protein + DNA
- Length
- 115 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ets translocation variant 5; 5'-D(*AP*CP*CP*GP*GP*AP*AP*GP*TP*GP)-3'…
- UniProt
- P41161
- Ligands
- CA
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 3 distinct chains · 48% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ets translocation variant 5 | protein | 95 | 48% helix, 13% strand | P41161 |
| B | 5'-D(*AP*CP*CP*GP*GP*AP*AP*GP*TP*GP)-3' | dna | 10 | — | — |
| C | 5'-D(*AP*CP*TP*TP*CP*CP*GP*GP*TP*CP)-3' | dna | 10 | — | — |
Ligands and binding sites
- CA · Calcium ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 62 | 0.38 | 0.79 | 13 | empty |
Interfaces
3 interfaces between chains.
- A–C · 534 Ų buried · 11 hydrogen bonds · protein-nucleic
- B–C · 401 Ų buried · 30 hydrogen bonds · nucleic-nucleic
- A–B · 376 Ų buried · 9 hydrogen bonds · protein-nucleic
Compared structures
- 4UNO · Crystal structure of the ETS domain of human ETV5 in complex with DNA · the same entry in another collection · chain A against A, TM-score 1.00
- P41161 · AlphaFold monomer V2.0 prediction for ets translocation variant 5 (P41161) · a predicted model of the same protein · chain A against A, TM-score 0.95
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 P41161
- Elsewhere: RCSB PDB 4UNO · PDBe 4UNO · UniProt P41161
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.