Research workbench
Structure of NEDD4L WW3 domain
Analyse Structure of NEDD4L WW3 domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7LP5
- Type
- protein
- Length
- 68 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ANGIOMOTIN,E3 ubiquitin-protein ligase NEDD4-like
- EC
- 2.3.2.26
- UniProt
- Q4VCS5, Q96PU5
Structure
solution nmr · 1 distinct chain · 10% helix, 19% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ANGIOMOTIN,E3 ubiquitin-protein ligase NEDD4-like (EC 2.3.2.26) | protein | 68 | 10% helix, 19% strand | Q4VCS5, Q96PU5 |
Compared structures
- 7LP5 · Structure of Nedd4L WW3 domain · 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 0.44
- Q4VCS5 · AlphaFold monomer V2.0 prediction for angiomotin (Q4VCS5) · a predicted model of the same protein · chain A against A, TM-score 0.21
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 Q4VCS5
- Every structure of UniProt Q96PU5
- Elsewhere: RCSB PDB 7LP5 · PDBe 7LP5 · UniProt Q4VCS5 · UniProt Q96PU5
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