Research workbench
UBE2D1 in complex with ubiquitin variant UBV.D1.1
Analyse UBE2D1 in complex with ubiquitin variant UBV.D1.1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6D4P
- Type
- protein
- Length
- 223 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ubiquitin-conjugating enzyme E2 D1; Ubiquitin variant UBV.D1.1
- EC
- 2.3.2.23, 2.3.2.24
- UniProt
- P51668, Q59EM9
- Pockets
- 1 · best druggability 0.52
Structure
x-ray diffraction · 2 distinct chains · 33% helix, 24% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ubiquitin-conjugating enzyme E2 D1 (EC 2.3.2.23, 2.3.2.24) | protein | 149 | 38% helix, 17% strand | P51668 |
| C | Ubiquitin variant UBV.D1.1 | protein | 74 | 24% helix, 38% strand | Q59EM9 |
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 126 | 0.52 | 0.81 | 21 | empty |
Interfaces
1 interface between chains.
- A–C · 792 Ų buried · 12 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 P51668
- Every structure of UniProt Q59EM9
- Elsewhere: RCSB PDB 6D4P · PDBe 6D4P · UniProt P51668 · UniProt Q59EM9
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