Research workbench
WW3 domain of NEDD4L in complex with its hect domain py motif
Analyse WW3 domain of NEDD4L in complex with its hect domain py motif in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2MPT
- Type
- protein
- Length
- 45 residues
- Chains
- 2
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase NEDD4-like
- EC
- 6.3.2.-
- UniProt
- Q96PU5
- Ligands
- NH2
Structure
solution nmr · 2 distinct chains · 0% helix, 29% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase NEDD4-like (EC 6.3.2.-) | protein | 32 | 0% helix, 41% strand | Q96PU5 |
| B | E3 ubiquitin-protein ligase NEDD4-like (EC 6.3.2.-) | protein | 13 | 0% helix, 0% strand | Q96PU5 |
Ligands and binding sites
- NH2 · Amino group · ion · chains B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Interfaces
1 interface between chains.
- A–B · 548 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 2MPT · WW3 domain of Nedd4L in complex with its HECT domain PY motif · 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 0.70
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 2MPT · PDBe 2MPT · UniProt Q96PU5
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