Research workbench
Double sided ubiquitin binding of hrs-uim
Analyse Double sided ubiquitin binding of hrs-uim in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2D3G
- Type
- protein
- Length
- 162 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin; Ubiquitin interacting motif from hepatocyte growth factor-regulated tyrosine…
- UniProt
- P62990, O14964
- Pockets
- 1 · best druggability 0.28
Structure
x-ray diffraction · 2 distinct chains · 38% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Ubiquitin | protein | 72 | 25% helix, 36% strand | P62990 |
| P | Ubiquitin interacting motif from hepatocyte growth factor-regulated tyrosine kinase substrate | protein | 18 | 89% helix, 0% strand | O14964 |
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 | 58 | 0.28 | 0.74 | 13 | empty |
Interfaces
3 interfaces between chains.
- A–P · 567 Ų buried · 5 hydrogen bonds · protein-protein
- B–P · 478 Ų buried · 2 hydrogen bonds · protein-protein
- A–B · 20 Ų buried · 0 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 P62990
- Every structure of UniProt O14964
- Elsewhere: RCSB PDB 2D3G · PDBe 2D3G · UniProt P62990 · UniProt O14964
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.