Research workbench
Crystal structure of the zalpha Z-DNA complex
Analyse Crystal structure of the zalpha Z-DNA complex in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 1QBJ
- Type
- protein + DNA
- Length
- 212 residues
- Chains
- 6
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DNA (5'-D(*TP*CP*GP*CP*GP*CP*G)-3'); Protein (double-stranded RNA specific adenosine…
- UniProt
- P55265
- Pockets
- 2 · best druggability 0.50
Structure
x-ray diffraction · 4 distinct chains · 56% helix, 13% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| D, E, F | DNA (5'-D(*TP*CP*GP*CP*GP*CP*G)-3') | dna | 6 | — | — |
| A | Protein (double-stranded RNA specific adenosine deaminase (ADAR1)) | protein | 65 | 57% helix, 14% strand | P55265 |
| B | Protein (double-stranded RNA specific adenosine deaminase (ADAR1)) | protein | 63 | 54% helix, 14% strand | P55265 |
| C | Protein (double-stranded RNA specific adenosine deaminase (ADAR1)) | protein | 66 | 58% helix, 12% strand | P55265 |
Pockets
2 pockets found on a 1 Å grid, 0 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 234 | 0.50 | 0.75 | 19 | empty |
| 2 | 191 | 0.49 | 0.77 | 24 | empty |
Interfaces
7 interfaces between chains.
- F–C · 428 Ų buried · 7 hydrogen bonds · protein-nucleic
- E–B · 427 Ų buried · 10 hydrogen bonds · protein-nucleic
- D–A · 404 Ų buried · 8 hydrogen bonds · protein-nucleic
- D–E · 326 Ų buried · 28 hydrogen bonds · nucleic-nucleic
- B–C · 184 Ų buried · 1 hydrogen bond · protein-protein
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 P55265
- Elsewhere: RCSB PDB 1QBJ · PDBe 1QBJ · UniProt P55265
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