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Crystal structure of free ERI2 nuclease
Analyse Crystal structure of free ERI2 nuclease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 7N8V
- Type
- protein
- Length
- 427 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- ERI1 exoribonuclease 2
- EC
- 3.1.-.-
- UniProt
- A8K979
- Ligands
- SO4
- Pockets
- 2 · best druggability 0.83
Structure
x-ray diffraction · 2 distinct chains · 39% helix, 20% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | ERI1 exoribonuclease 2 (EC 3.1.-.-) | protein | 214 | 39% helix, 20% strand | A8K979 |
| B | ERI1 exoribonuclease 2 (EC 3.1.-.-) | protein | 213 | 38% helix, 20% strand | A8K979 |
Ligands and binding sites
- SO4 · Sulfate ion · ion · 4 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, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1128 | 0.83 | 0.84 | 101 | SO4 |
| 2 | 142 | 0.56 | 0.83 | 31 | SO4 |
Interfaces
1 interface between chains.
- A–B · 889 Ų buried · 8 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 A8K979
- Elsewhere: RCSB PDB 7N8V · PDBe 7N8V · UniProt A8K979
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