Research workbench
Zinc-dependent bifunctional nuclease
Analyse Zinc-dependent bifunctional nuclease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3W52
- Type
- protein
- Length
- 256 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v2 / PDB Bank
- Contract
- 0xd58B01f6C18086e5202cdC5D7Ad3E41790360102
- Owner
- 0xF4e1AA6f26B7DA48EeAD9B24a97927303eeA07b8
- Resolution
- 1.76
- Source
- Arabidopsis thaliana
- Molecule
- Endonuclease 2
- EC
- 3.1.30.1
- UniProt
- Q9C9G4
- Ligands
- ADE, NAG, BMA, ZN, SO4
- Pockets
- 1 · best druggability 0.33
Structure
x-ray diffraction · resolution 1.76 · 1 distinct chain · 63% helix, 7% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endonuclease 2 (EC 3.1.30.1) | protein | 256 | 63% helix, 7% strand | Q9C9G4 |
Ligands and binding sites
- ADE · Adenine · ligand · chains A
- NAG · 2-acetamido-2-deoxy-beta-D-glucopyranose · sugar · 6 copies · chains A
- BMA · beta-D-mannopyranose · sugar · chains A
- ZN · Zinc ion · metal · 3 copies · chains A
- SO4 · Sulfate ion · ion · 3 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 | 63 | 0.33 | 0.77 | 24 | ADE, ZN, SO4 |
Modifications
Observed in the structure: 4 disulfide, 3 glycan (disulfide, N-glycosylation).
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 Q9C9G4
- Elsewhere: RCSB PDB 3W52 · PDBe 3W52 · UniProt Q9C9G4
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