Research workbench
E3 ring ligase binding domain
Analyse E3 ring ligase binding domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7OVX
- Type
- protein
- Length
- 186 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase TRIM7; Peptide G
- EC
- 2.3.2.27
- UniProt
- Q9C029
- Pockets
- 1 · best druggability 0.30
Structure
x-ray diffraction · 2 distinct chains · 8% helix, 40% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase TRIM7 (EC 2.3.2.27) | protein | 174 | 3% helix, 43% strand | Q9C029 |
| Q | Peptide G | protein | 12 | 67% helix, 0% strand | — |
Pockets
1 pocket found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 78 | 0.30 | 0.73 | 16 | empty |
Interfaces
1 interface between chains.
- A–Q · 490 Ų buried · 16 hydrogen bonds · 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 Q9C029
- Elsewhere: RCSB PDB 7OVX · PDBe 7OVX · UniProt Q9C029
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