Research workbench
Crystal structure of the C2 domain of the human E3 ubiquitin-protein ligase NEDD4-like protein
Analyse Crystal structure of the C2 domain of the human E3 ubiquitin-protein ligase… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2NSQ
- Type
- protein
- Length
- 140 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase NEDD4-like protein
- EC
- 6.3.2.-
- UniProt
- Q96PU5
Structure
x-ray diffraction · 1 distinct chain · 0% helix, 51% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase NEDD4-like protein (EC 6.3.2.-) | protein | 140 | 0% helix, 51% strand | Q96PU5 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 2NSQ · Crystal structure of the C2 domain of the human E3 ubiquitin-protein ligase NEDD4-like… · the same entry in another collection · chain A against A, TM-score 1.00
- Q96PU5 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase NEDD4-like (Q96PU5) · a predicted model of the same protein · chain A against A, TM-score 0.94
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 Q96PU5
- Elsewhere: RCSB PDB 2NSQ · PDBe 2NSQ · UniProt Q96PU5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.