Research workbench
Extracellular endonuclease
Analyse Extracellular endonuclease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2XGR
- Type
- protein
- Length
- 197 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- SPD1 nuclease
- EC
- 3.1.21.1
- UniProt
- Q9A0M1
- Pockets
- 3 · best druggability 0.49
Structure
x-ray diffraction · 1 distinct chain · 16% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | SPD1 nuclease (EC 3.1.21.1) | protein | 197 | 16% helix, 31% strand | Q9A0M1 |
Ligands and binding sites
- PEG · Di(hydroxyethyl)ether · additive · 8 copies · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 173 | 0.49 | 0.77 | 22 | PEG |
| 2 | 55 | 0.33 | 0.77 | 18 | empty |
| 3 | 53 | 0.30 | 0.75 | 17 | empty |
Compared structures
- 2XGR · extracellular endonuclease · the same entry in another collection · chain A against A, 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 Q9A0M1
- Elsewhere: RCSB PDB 2XGR · PDBe 2XGR · UniProt Q9A0M1
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