Research workbench
Crystal Structure of a Functionally Uncharacterized Domain of E3 Ubiquitin Ligase SHPRH
Analyse Crystal Structure of a Functionally Uncharacterized Domain of E3 Ubiquitin… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QN1
- Type
- protein
- Length
- 372 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.48
- Source
- Homo sapiens
- Molecule
- E3 ubiquitin-protein ligase SHPRH
- UniProt
- Q149N8
- Ligands
- ZN, SO4, UNX
- Pockets
- 3 · best druggability 0.52
Structure
x-ray diffraction · resolution 2.48 · 1 distinct chain · 76% helix, 2% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | E3 ubiquitin-protein ligase SHPRH | protein | 372 | 76% helix, 2% strand | Q149N8 |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
- SO4 · Sulfate ion · ion · chains A
- UNX · Unknown atom or ion · ion · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 139 | 0.52 | 0.80 | 20 | empty |
| 2 | 138 | 0.44 | 0.76 | 21 | empty |
| 3 | 69 | 0.34 | 0.76 | 16 | empty |
Modifications
Observed in the structure: 9 modified (engineered).
Compared structures
- 4QN1 · Crystal structure of a functionally uncharacterized domain of E3 ubiquitin ligase shprh · the same entry in another collection · chain A against A, TM-score 1.00
- Q149N8 · AlphaFold monomer V2.0 prediction for E3 ubiquitin-protein ligase shprh (Q149N8) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q149N8
- Elsewhere: RCSB PDB 4QN1 · PDBe 4QN1 · UniProt Q149N8
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