Research workbench
Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 hect domain E3 ligase
Analyse Conformational flexibility underlies ubiquitin ligation mediated by the WWP1… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1ND7
- Type
- protein
- Length
- 374 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Ww domain-containing protein 1
- UniProt
- Q9H0M0
- Pockets
- 3 · best druggability 0.79
Structure
x-ray diffraction · 1 distinct chain · 49% helix, 11% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ww domain-containing protein 1 | protein | 374 | 49% helix, 11% strand | Q9H0M0 |
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 711 | 0.79 | 0.84 | 80 | empty |
| 2 | 70 | 0.36 | 0.77 | 20 | empty |
| 3 | 105 | 0.35 | 0.74 | 18 | empty |
Compared structures
- 1ND7 · Conformational Flexibility Underlies Ubiquitin Ligation Mediated by the WWP1 HECT domain… · the same entry in another collection · chain A against A, TM-score 1.00
- Q9H0M0 · AlphaFold monomer V2.0 prediction for NEDD4-like E3 ubiquitin-protein ligase WWP1 (Q9H0M0) · a predicted model of the same protein · chain A against A, TM-score 0.96
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 Q9H0M0
- Elsewhere: RCSB PDB 1ND7 · PDBe 1ND7 · UniProt Q9H0M0
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