MolNFT v1 · #45173 · protein
The proteolytic activity of ubiquitin-specific protease 28 is modulated by the N-terminal domain
2MUU: “The proteolytic activity of ubiquitin-specific protease 28 is modulated by the N-terminal domain”. Solution nmr. MolNFT v1 #45173 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 2MUU
- Type
- protein
- Length
- 120 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q96RU2
Structure
solution nmr · 1 distinct chain.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 120 | — | Q96RU2 |
Compared structures
- 2MUU · The Proteolytic Activity of Ubiquitin-specific Protease 28 Is Modulated by the N-terminal… · the same entry in another collection · chain A against A, TM-score 1.00
- Q96RU2 · AlphaFold monomer V2.0 prediction for ubiquitin carboxyl-terminal hydrolase 28 (Q96RU2) · a predicted model of the same protein · chain A against A, TM-score 0.43
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 Q96RU2
- Elsewhere: RCSB PDB 2MUU · PDBe 2MUU · UniProt Q96RU2
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