Research workbench
Structure analysis of function associated loop mutant of substrate recognition domain of FBS1 ubiquitin ligase
Analyse Structure analysis of function associated loop mutant of substrate recognition… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5B4N
- Type
- protein
- Length
- 348 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- F-box only protein 2
- UniProt
- Q80UW2
- Pockets
- 2 · best druggability 0.69
Structure
x-ray diffraction · 1 distinct chain · 9% helix, 41% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | F-box only protein 2 | protein | 174 | 9% helix, 41% strand | Q80UW2 |
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 246 | 0.69 | 0.85 | 48 | empty |
| 2 | 80 | 0.35 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 721 Ų buried · 17 hydrogen bonds · protein-protein
Compared structures
- 5B4N · Structure analysis of function associated loop mutant of substrate recognition domain of… · the same entry in another collection · chain A against A, TM-score 1.00
- Q80UW2 · AlphaFold monomer V2.0 prediction for F-box only protein 2 (Q80UW2) · a predicted model of the same protein · chain B against A, TM-score 0.87
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 Q80UW2
- Elsewhere: RCSB PDB 5B4N · PDBe 5B4N · UniProt Q80UW2
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.