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
- 7LP2
- Type
- protein
- Length
- 141 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase; Angiomotin
- EC
- 2.3.2.26
- UniProt
- A0A6Q8PG51, Q4VCS5
- Ligands
- SO4
- Pockets
- 1 · best druggability 0.65
Structure
x-ray diffraction · 5 distinct chains · 8% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, C | E3 ubiquitin-protein ligase (EC 2.3.2.26) | protein | 33 | 0% helix, 42% strand | A0A6Q8PG51 |
| B | Angiomotin | protein | 11 | 27% helix, 0% strand | Q4VCS5 |
| D | Angiomotin | protein | 12 | 25% helix, 0% strand | Q4VCS5 |
| E | E3 ubiquitin-protein ligase (EC 2.3.2.26) | protein | 37 | 0% helix, 35% strand | A0A6Q8PG51 |
| F | Angiomotin | protein | 15 | 20% helix, 0% strand | Q4VCS5 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 copies · chains E, F, D
- GOL · Glycerol · additive · 2 copies · chains C, E
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 103 | 0.65 | 0.89 | 36 | empty |
Interfaces
11 interfaces between chains.
- E–F · 552 Ų buried · 7 hydrogen bonds · protein-protein
- A–C · 529 Ų buried · 9 hydrogen bonds · protein-protein
- C–D · 489 Ų buried · 5 hydrogen bonds · protein-protein
- A–B · 382 Ų buried · 4 hydrogen bonds · protein-protein
- A–F · 327 Ų buried · 1 hydrogen bond · 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 A0A6Q8PG51
- Every structure of UniProt Q4VCS5
- Elsewhere: RCSB PDB 7LP2 · PDBe 7LP2 · UniProt A0A6Q8PG51 · UniProt Q4VCS5
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.