Research workbench
Crystal structure of ELP2
Analyse Crystal structure of ELP2 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4XFV
- Type
- protein
- Length
- 700 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Elongator complex protein 2
- UniProt
- P42935
- Pockets
- 6 · best druggability 0.77
Structure
x-ray diffraction · 1 distinct chain · 2% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Elongator complex protein 2 | protein | 700 | 2% helix, 51% strand | P42935 |
Pockets
6 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 821 | 0.77 | 0.81 | 70 | empty |
| 2 | 334 | 0.71 | 0.84 | 32 | empty |
| 3 | 57 | 0.66 | 0.95 | 26 | empty |
| 4 | 204 | 0.58 | 0.81 | 20 | empty |
| 5 | 81 | 0.44 | 0.80 | 25 | empty |
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 P42935
- Elsewhere: RCSB PDB 4XFV · PDBe 4XFV · UniProt P42935
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.