Research workbench
Crystal structure of apo noti restriction endonuclease
Analyse Crystal structure of apo noti restriction endonuclease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3BVQ
- Type
- protein
- Length
- 694 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Noti restriction endonuclease
- UniProt
- Q2I6W2
- Ligands
- FE, SO4
- Pockets
- 9 · best druggability 0.62
Structure
x-ray diffraction · 2 distinct chains · 34% helix, 22% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Noti restriction endonuclease | protein | 342 | 33% helix, 22% strand | Q2I6W2 |
| B | Noti restriction endonuclease | protein | 352 | 34% helix, 23% strand | Q2I6W2 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 216 | 0.62 | 0.82 | 25 | empty |
| 2 | 288 | 0.55 | 0.76 | 30 | SO4 |
| 3 | 201 | 0.53 | 0.78 | 26 | empty |
| 4 | 294 | 0.53 | 0.75 | 36 | SO4 |
| 5 | 86 | 0.49 | 0.82 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 3407 Ų buried · 28 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 10 modified (engineered).
Compared structures
- 3BVQ · Crystal Structure of Apo NotI Restriction 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 Q2I6W2
- Elsewhere: RCSB PDB 3BVQ · PDBe 3BVQ · UniProt Q2I6W2
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