Research workbench
Drosophila unr CSD456
Analyse Drosophila unr CSD456 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6Y6E
- Type
- protein
- Length
- 238 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Upstream of N-RAS, isoform a
- UniProt
- Q9VSK3
- Ligands
- EMC
- Pockets
- 2 · best druggability 0.31
Structure
x-ray diffraction · 1 distinct chain · 7% helix, 50% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Upstream of N-RAS, isoform a | protein | 238 | 7% helix, 50% strand | Q9VSK3 |
Ligands and binding sites
- EMC · Ethyl mercury ion · metal · 4 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 69 | 0.31 | 0.74 | 17 | empty |
| 2 | 61 | 0.29 | 0.74 | 13 | empty |
Compared structures
- 6Y6E · drosophila Unr CSD456 · the same entry in another collection · chain A against A, TM-score 1.00
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 Q9VSK3
- Elsewhere: RCSB PDB 6Y6E · PDBe 6Y6E · UniProt Q9VSK3
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