Research workbench
Nemo cozi domain
Analyse Nemo cozi domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3F89
- Type
- protein
- Length
- 165 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nf-kappa-B essential modulator
- UniProt
- O88522
Structure
x-ray diffraction · 2 distinct chains · 87% helix, 0% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Nf-kappa-B essential modulator | protein | 83 | 83% helix, 0% strand | O88522 |
| B | Nf-kappa-B essential modulator | protein | 82 | 91% helix, 0% strand | O88522 |
Interfaces
1 interface between chains.
- A–B · 2219 Ų buried · 9 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 O88522
- Elsewhere: RCSB PDB 3F89 · PDBe 3F89 · UniProt O88522
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.