Research workbench
Apo crystal structure of the homing endonuclease, I-ppoi
Analyse Apo crystal structure of the homing endonuclease, I-ppoi in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1EVX
- Type
- protein
- Length
- 324 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Intron-encoded homing endonuclease I-ppoi
- UniProt
- Q94702
- Ligands
- ZN, SO4
- Pockets
- 3 · best druggability 0.64
Structure
x-ray diffraction · 1 distinct chain · 19% helix, 31% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Intron-encoded homing endonuclease I-ppoi | protein | 162 | 19% helix, 31% strand | Q94702 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
3 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 108 | 0.64 | 0.89 | 31 | empty |
| 2 | 92 | 0.35 | 0.75 | 19 | SO4 |
| 3 | 92 | 0.34 | 0.74 | 21 | SO4 |
Interfaces
1 interface between chains.
- A–B · 2472 Ų buried · 38 hydrogen bonds · protein-protein
Compared structures
- 1EVX · Apo crystal structure of the homing endonuclease, I-ppoi · the same entry in another collection · chain A against A, TM-score 1.00
- Q94702 · AlphaFold monomer V2.0 prediction for intron-encoded endonuclease I-ppoi (Q94702) · a predicted model of the same protein · chain A against A, TM-score 0.97
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 Q94702
- Elsewhere: RCSB PDB 1EVX · PDBe 1EVX · UniProt Q94702
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