Research workbench
Thermus thermophilus ruvc structure
Analyse Thermus thermophilus ruvc structure in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4EP4
- Type
- protein
- Length
- 332 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Crossover junction endodeoxyribonuclease ruvc
- EC
- 3.1.22.4
- UniProt
- Q5SJC4
- Ligands
- MG
- Pockets
- 4 · best druggability 0.60
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 21% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Crossover junction endodeoxyribonuclease ruvc (EC 3.1.22.4) | protein | 166 | 46% helix, 21% strand | Q5SJC4 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 162 | 0.60 | 0.83 | 19 | MG |
| 2 | 67 | 0.51 | 0.86 | 19 | empty |
| 3 | 105 | 0.44 | 0.78 | 23 | empty |
| 4 | 54 | 0.31 | 0.76 | 17 | empty |
Interfaces
1 interface between chains.
- A–B · 1267 Ų buried · 10 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 Q5SJC4
- Elsewhere: RCSB PDB 4EP4 · PDBe 4EP4 · UniProt Q5SJC4
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