Research workbench
Crystal structure of the refolded DENV3 methyltransferase
Analyse Crystal structure of the refolded DENV3 methyltransferase in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4R05
- Type
- protein
- Length
- 514 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Nonstructural protein NS5
- UniProt
- C1KBQ3
- Pockets
- 5 · best druggability 0.73
Structure
x-ray diffraction · 1 distinct chain · 37% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A, B | Nonstructural protein NS5 | protein | 257 | 37% helix, 16% strand | C1KBQ3 |
Pockets
5 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 915 | 0.73 | 0.77 | 81 | empty |
| 2 | 621 | 0.67 | 0.76 | 51 | empty |
| 3 | 115 | 0.41 | 0.76 | 24 | empty |
| 4 | 73 | 0.36 | 0.77 | 22 | empty |
| 5 | 51 | 0.30 | 0.76 | 12 | empty |
Interfaces
1 interface between chains.
- A–B · 601 Ų buried · 6 hydrogen bonds · protein-protein
Compared structures
- 4R05 · Crystal structure of the refolded DENV3 methyltransferase · 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 C1KBQ3
- Elsewhere: RCSB PDB 4R05 · PDBe 4R05 · UniProt C1KBQ3
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