Research workbench
RING1B-BMI1 fusion in closed conformation
Analyse RING1B-BMI1 fusion in closed conformation in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6WI7
- Type
- protein
- Length
- 206 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase RING2, polycomb complex protein bmi-1 chimera
- EC
- 5.-.-.-
- UniProt
- X6RFN3, P35226
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.38
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase RING2, polycomb complex protein bmi-1 chimera (EC 5.-.-.-) | protein | 206 | 37% helix, 17% strand | X6RFN3, P35226 |
Ligands and binding sites
- ZN · Zinc ion · metal · 4 copies · chains A
- EPE · 4-(2-hydroxyethyl)-1-piperazine ethanesulfonic acid · additive · chains A
- GOL · Glycerol · additive · 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 | 73 | 0.38 | 0.77 | 21 | 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 X6RFN3
- Every structure of UniProt P35226
- Elsewhere: RCSB PDB 6WI7 · PDBe 6WI7 · UniProt X6RFN3 · UniProt P35226
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