Research workbench
VRR_NUC domain
Analyse VRR_NUC domain in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4QBN
- Type
- protein
- Length
- 186 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nuclease
- UniProt
- A3EZR7
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 44% helix, 25% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Nuclease | protein | 93 | 44% helix, 25% strand | A3EZR7 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 6 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
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 | 231 | 0.52 | 0.76 | 28 | SO4 |
| 2 | 199 | 0.49 | 0.76 | 25 | empty |
Interfaces
1 interface between chains.
- A–B · 375 Ų buried · 1 hydrogen bond · protein-protein
Compared structures
- 4QBN · VRR_NUC domain · the same entry in another collection · chain B against B, TM-score 1.00
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 A3EZR7
- Elsewhere: RCSB PDB 4QBN · PDBe 4QBN · UniProt A3EZR7
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