Research workbench
Solution structure of the ring domain of the E3 ubiquitin ligase HRD1
Analyse Solution structure of the ring domain of the E3 ubiquitin ligase HRD1 in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6F98
- Type
- protein
- Length
- 78 residues
- Chains
- 1
- Method
- solution nmr
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase
- UniProt
- A0A250WAY8
- Ligands
- ZN
- Pockets
- 1 · best druggability 0.35
Structure
solution nmr · 1 distinct chain · 14% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase | protein | 78 | 14% helix, 13% strand | A0A250WAY8 |
Ligands and binding sites
- ZN · Zinc ion · metal · 2 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 61 | 0.35 | 0.77 | 15 | empty |
Compared structures
- 6F98 · Solution structure of the RING domain of the E3 ubiquitin ligase HRD1 · the same entry in another collection · chain A against A, TM-score 1.00
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 A0A250WAY8
- Elsewhere: RCSB PDB 6F98 · PDBe 6F98 · UniProt A0A250WAY8
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