Research workbench
Ubiquitin binding variants
Analyse Ubiquitin binding variants in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6NXK
- Type
- protein
- Length
- 296 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Polyubiquitin-C; Anaphase-promoting complex subunit 2
- UniProt
- P0CG48, Q9UJX6
- Pockets
- 3 · best druggability 0.51
Structure
x-ray diffraction · 3 distinct chains · 51% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Polyubiquitin-C | protein | 73 | 25% helix, 34% strand | P0CG48 |
| C | Anaphase-promoting complex subunit 2 | protein | 76 | 62% helix, 9% strand | Q9UJX6 |
| D | Anaphase-promoting complex subunit 2 | protein | 74 | 66% helix, 11% strand | Q9UJX6 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 175 | 0.51 | 0.77 | 27 | empty |
| 2 | 104 | 0.44 | 0.78 | 16 | empty |
| 3 | 55 | 0.32 | 0.76 | 10 | empty |
Interfaces
5 interfaces between chains.
- A–C · 485 Ų buried · 6 hydrogen bonds · protein-protein
- B–D · 436 Ų buried · 6 hydrogen bonds · protein-protein
- C–D · 383 Ų buried · 0 hydrogen bonds · protein-protein
- B–C · 366 Ų buried · 2 hydrogen bonds · protein-protein
- A–D · 288 Ų buried · 2 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 P0CG48
- Every structure of UniProt Q9UJX6
- Elsewhere: RCSB PDB 6NXK · PDBe 6NXK · UniProt P0CG48 · UniProt Q9UJX6
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