Research workbench
Structure and ubiquitin interactions of the conserved nzf domain of NPL4
Analyse Structure and ubiquitin interactions of the conserved nzf domain of NPL4 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1NJ3
- Type
- protein
- Length
- 31 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- NPL4
- UniProt
- Q9ES54
- Ligands
- ZN
Structure
solution nmr · 1 distinct chain · 0% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | NPL4 | protein | 31 | 0% helix, 13% strand | Q9ES54 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 1NJ3 · Structure and Ubiquitin Interactions of the Conserved NZF Domain of Npl4 · the same entry in another collection · chain A against A, TM-score 1.00
- Q9ES54 · AlphaFold monomer V2.0 prediction for nuclear protein localization protein 4 homolog… · a predicted model of the same protein · chain A against A, TM-score 0.65
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 Q9ES54
- Elsewhere: RCSB PDB 1NJ3 · PDBe 1NJ3 · UniProt Q9ES54
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