Research workbench
Crystal structure of a C-tagged nuclease
Analyse Crystal structure of a C-tagged nuclease in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4O88
- Type
- protein
- Length
- 630 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- N-tagged nuclease
- UniProt
- Q707V3
- Ligands
- SO4, CL
- Pockets
- 4 · best druggability 0.61
Structure
x-ray diffraction · 2 distinct chains · 50% helix, 14% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | N-tagged nuclease | protein | 316 | 51% helix, 13% strand | Q707V3 |
| B | N-tagged nuclease | protein | 314 | 50% helix, 15% strand | Q707V3 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 386 | 0.61 | 0.77 | 43 | CL, SO4 |
| 2 | 335 | 0.59 | 0.77 | 38 | CL |
| 3 | 185 | 0.49 | 0.76 | 26 | empty |
| 4 | 79 | 0.40 | 0.78 | 18 | empty |
Interfaces
1 interface between chains.
- A–B · 113 Ų buried · 0 hydrogen bonds · protein-protein
Compared structures
- 4O88 · Crystal structure of a C-tagged Nuclease · 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 Q707V3
- Elsewhere: RCSB PDB 4O88 · PDBe 4O88 · UniProt Q707V3
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