Research workbench
The 1.6 a crystal structure of vibrio cholerae extracellular endonuclease I
Analyse The 1.6 a crystal structure of vibrio cholerae extracellular endonuclease I in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2G7E
- Type
- protein
- Length
- 207 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Endonuclease I
- EC
- 3.1.21.1
- UniProt
- Q2XSK9
- Ligands
- CL
- Pockets
- 2 · best druggability 0.52
Structure
x-ray diffraction · 1 distinct chain · 52% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Endonuclease I (EC 3.1.21.1) | protein | 207 | 52% helix, 18% strand | Q2XSK9 |
Ligands and binding sites
- CL · Chloride ion · ion · chains A
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 | 102 | 0.52 | 0.83 | 26 | empty |
| 2 | 96 | 0.34 | 0.74 | 26 | empty |
Modifications
Observed in the structure: 4 disulfide (disulfide).
Compared structures
- 2G7E · The 1.6 A crystal structure of Vibrio cholerae extracellular endonuclease I · 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 Q2XSK9
- Elsewhere: RCSB PDB 2G7E · PDBe 2G7E · UniProt Q2XSK9
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