Research workbench
Mouse NP95 sra domain non-specific DNA complex
Analyse Mouse NP95 sra domain non-specific DNA complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 2ZO2
- Type
- protein + DNA
- Length
- 225 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- E3 ubiquitin-protein ligase UHRF1; DNA (5'- D(*DAP*DAP*DCP*DTP*DGP*DCP*DGP*DCP*DAP*DGP*DTP…
- EC
- 6.3.2.-
- UniProt
- Q8VDF2
- Ligands
- PO4
- Pockets
- 3 · best druggability 0.59
Structure
x-ray diffraction · 2 distinct chains · 20% helix, 26% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| B | E3 ubiquitin-protein ligase UHRF1 (EC 6.3.2.-) | protein | 201 | 20% helix, 26% strand | Q8VDF2 |
| D, E | DNA (5'- D(*DAP*DAP*DCP*DTP*DGP*DCP*DGP*DCP*DAP*DGP*DTP*DT)-3') | dna | 12 | — | — |
Ligands and binding sites
- PO4 · Phosphate ion · ion · chains B
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 | 266 | 0.59 | 0.79 | 39 | empty |
| 2 | 69 | 0.28 | 0.73 | 10 | empty |
| 3 | 56 | 0.26 | 0.73 | 13 | empty |
Interfaces
2 interfaces between chains.
- D–E · 557 Ų buried · 39 hydrogen bonds · nucleic-nucleic
- B–E · 277 Ų buried · 1 hydrogen bond · protein-nucleic
Compared structures
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 Q8VDF2
- Elsewhere: RCSB PDB 2ZO2 · PDBe 2ZO2 · UniProt Q8VDF2
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