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Crystal structure of UfSP from C.elegans
Analyse Crystal structure of UfSP from C.elegans in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5EJJ
- Type
- protein
- Length
- 1,037 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 2.8
- Source
- Caenorhabditis elegans
- Molecule
- Ufm1-specific protease
- EC
- 3.4.22.-
- UniProt
- Q94218
- Pockets
- 12 · best druggability 0.77
Structure
x-ray diffraction · resolution 2.8 · 2 distinct chains · 31% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Ufm1-specific protease (EC 3.4.22.-) | protein | 517 | 31% helix, 25% strand | Q94218 |
| B | Ufm1-specific protease (EC 3.4.22.-) | protein | 520 | 31% helix, 25% strand | Q94218 |
Pockets
12 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 356 | 0.77 | 0.88 | 43 | empty |
| 2 | 957 | 0.76 | 0.79 | 88 | empty |
| 3 | 573 | 0.69 | 0.78 | 48 | empty |
| 4 | 85 | 0.52 | 0.84 | 21 | empty |
| 5 | 139 | 0.47 | 0.77 | 21 | empty |
Interfaces
1 interface between chains.
- A–B · 976 Ų buried · 13 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 Q94218
- Elsewhere: RCSB PDB 5EJJ · PDBe 5EJJ · UniProt Q94218
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