Research workbench
Crystal structure of the murine DHX36 helicase in complex with ADP
Analyse Crystal structure of the murine DHX36 helicase in complex with ADP in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 6UP4
- Type
- protein
- Length
- 814 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- DHX36 protein
- UniProt
- B2RQS6
- Ligands
- ADP, MG
- Pockets
- 9 · best druggability 0.82
Structure
x-ray diffraction · 1 distinct chain · 46% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | DHX36 protein | protein | 814 | 46% helix, 17% strand | B2RQS6 |
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, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 512 | 0.82 | 0.89 | 71 | empty |
| 2 | 212 | 0.73 | 0.89 | 27 | empty |
| 3 | 359 | 0.70 | 0.83 | 36 | ADP, MG |
| 4 | 281 | 0.67 | 0.83 | 46 | empty |
| 5 | 253 | 0.61 | 0.80 | 26 | empty |
Compared structures
- 6UP4 · Crystal structure of the murine DHX36 helicase in complex with ADP · 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 B2RQS6
- Elsewhere: RCSB PDB 6UP4 · PDBe 6UP4 · UniProt B2RQS6
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