Research workbench
SUMO2 non-covalently interacts with USP25 and downregulates its activity
Analyse SUMO2 non-covalently interacts with USP25 and downregulates its activity in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MUX
- Type
- protein
- Length
- 146 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q9UHP3
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 146 | — | Q9UHP3 |
Compared structures
- 2MUX · SUMO2 non-covalently interacts with USP25 and downregulates its activity · the same entry in another collection · chain A against A, TM-score 1.00
- Q9UHP3 · AlphaFold monomer V2.0 prediction for ubiquitin carboxyl-terminal hydrolase 25 (Q9UHP3) · a predicted model of the same protein · chain A against A, TM-score 0.31
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 Q9UHP3
- Elsewhere: RCSB PDB 2MUX · PDBe 2MUX · UniProt Q9UHP3
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