Research workbench
Crystal structure of the DNA-binding domain of human ETV1.
Analyse Crystal structure of the DNA-binding domain of human ETV1. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4AVP
- Type
- protein
- Length
- 372 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ets translocation variant 1
- UniProt
- P50549
- Pockets
- 1 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 15% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B, C, D | Ets translocation variant 1 | protein | 93 | 49% helix, 15% strand | P50549 |
Ligands and binding sites
- EDO · 1,2-ethanediol · additive · 2 copies · chains B, D
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 819 | 0.73 | 0.78 | 87 | empty |
Interfaces
5 interfaces between chains.
- C–D · 854 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 843 Ų buried · 2 hydrogen bonds · protein-protein
- A–C · 372 Ų buried · 3 hydrogen bonds · protein-protein
- B–D · 337 Ų buried · 1 hydrogen bond · protein-protein
- B–C · 31 Ų buried · 0 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 P50549
- Elsewhere: RCSB PDB 4AVP · PDBe 4AVP · UniProt P50549
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