MolNFT v1 · #54921 · protein
RAD18 ubiquitin ligase ring domain structure
2Y43 · E3 ubiquitin-protein ligase RAD18: “RAD18 ubiquitin ligase ring domain structure”. X-ray diffraction, 1 ligand (ZN), 2 pockets (best druggability 0.32). MolNFT v1 #54921 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2Y43
- Type
- protein
- Length
- 176 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase RAD18
- EC
- 6.3.2.-
- UniProt
- Q9NS91
- Ligands
- ZN
- Pockets
- 2 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 42% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase RAD18 (EC 6.3.2.-) | protein | 88 | 43% helix, 14% strand | Q9NS91 |
| B | E3 ubiquitin-protein ligase RAD18 (EC 6.3.2.-) | protein | 88 | 41% helix, 14% strand | Q9NS91 |
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
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 | 77 | 0.32 | 0.74 | 14 | empty |
| 2 | 59 | 0.26 | 0.72 | 15 | empty |
Interfaces
1 interface between chains.
- A–B · 1131 Ų buried · 6 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 Q9NS91
- Elsewhere: RCSB PDB 2Y43 · PDBe 2Y43 · UniProt Q9NS91
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.