Research workbench
Disulfide between ubiquitin G76C and the E3 hect ligase HUWE1
Analyse Disulfide between ubiquitin G76C and the E3 hect ligase HUWE1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6FYH
- Type
- protein
- Length
- 191 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase HUWE1; Polyubiquitin-B
- EC
- 2.3.2.26
- UniProt
- Q7Z6Z7, P0CG47
- Ligands
- ZN, SO4
- Pockets
- 2 · best druggability 0.32
Structure
x-ray diffraction · 2 distinct chains · 30% helix, 23% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase HUWE1 (EC 2.3.2.26) | protein | 115 | 37% helix, 17% strand | Q7Z6Z7 |
| B | Polyubiquitin-B | protein | 76 | 20% helix, 33% strand | P0CG47 |
Ligands and binding sites
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 | 50 | 0.32 | 0.77 | 15 | empty |
| 2 | 52 | 0.27 | 0.73 | 10 | empty |
Interfaces
1 interface between chains.
- A–B · 587 Ų buried · 11 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 6FYH · Disulfide between ubiquitin G76C and the E3 HECT ligase Huwe1 · 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 Q7Z6Z7
- Every structure of UniProt P0CG47
- Elsewhere: RCSB PDB 6FYH · PDBe 6FYH · UniProt Q7Z6Z7 · UniProt P0CG47
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