Research workbench
Crystal structure of USP30 in covalent complex with ubiquitin propargylamide (high resolution)
Analyse Crystal structure of USP30 in covalent complex with ubiquitin propargylamide… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5OHK
- Type
- protein
- Length
- 379 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- Q70CQ3, P0CG47
- Ligands
- AYE, ZN
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 304 | — | Q70CQ3 |
| B | — | protein | 75 | — | P0CG47 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5OHK · Crystal structure of USP30 in covalent complex with ubiquitin propargylamide (high… · the same entry in another collection · chain A against A, TM-score 1.00
- Q70CQ3 · AlphaFold monomer V2.0 prediction for ubiquitin carboxyl-terminal hydrolase 30 (Q70CQ3) · a predicted model of the same protein · chain A against A, TM-score 0.98
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 Q70CQ3
- Every structure of UniProt P0CG47
- Elsewhere: RCSB PDB 5OHK · PDBe 5OHK · UniProt Q70CQ3 · UniProt P0CG47
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