Research workbench
Crystal structure of drosophilia DHX36 helicase in complex with gagcactgc
Analyse Crystal structure of drosophilia DHX36 helicase in complex with gagcactgc in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5N8R
- Type
- protein + DNA
- Length
- 1,718 residues
- Chains
- 4
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- CG9323, isoform a; DNA (5'-D(P*GP*AP*GP*CP*AP*CP*TP*GP*C)-3')
- EC
- 3.6.1.3
- UniProt
- Q8SWT2
- Pockets
- 20 · best druggability 0.87
Structure
x-ray diffraction · 3 distinct chains · 48% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | CG9323, isoform a (EC 3.6.1.3) | protein | 849 | 48% helix, 16% strand | Q8SWT2 |
| B | CG9323, isoform a (EC 3.6.1.3) | protein | 851 | 48% helix, 17% strand | Q8SWT2 |
| C, D | DNA (5'-D(P*GP*AP*GP*CP*AP*CP*TP*GP*C)-3') | dna | 9 | — | — |
Pockets
20 pockets found on a 1 Å grid, 17 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 791 | 0.87 | 0.90 | 79 | empty |
| 2 | 451 | 0.82 | 0.90 | 33 | empty |
| 3 | 538 | 0.82 | 0.89 | 59 | empty |
| 4 | 789 | 0.82 | 0.85 | 74 | empty |
| 5 | 217 | 0.77 | 0.92 | 23 | empty |
Interfaces
3 interfaces between chains.
- A–C · 1555 Ų buried · 31 hydrogen bonds · protein-nucleic
- B–D · 1551 Ų buried · 34 hydrogen bonds · protein-nucleic
- A–B · 479 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 5N8R · Crystal Structure of Drosophilia DHX36 helicase in complex with GAGCACTGC · 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 Q8SWT2
- Elsewhere: RCSB PDB 5N8R · PDBe 5N8R · UniProt Q8SWT2
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