Research workbench
Crystal structure of the zika virus NS5 methyltransferase.
Analyse Crystal structure of the zika virus NS5 methyltransferase. in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 5VIM
- Type
- protein
- Length
- 523 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Methyltransferase
- UniProt
- A0A192GPS6
- Ligands
- SAM, SO4
- Pockets
- 2 · best druggability 0.71
Structure
x-ray diffraction · 2 distinct chains · 37% helix, 17% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Methyltransferase | protein | 261 | 37% helix, 17% strand | A0A192GPS6 |
| B | Methyltransferase | protein | 262 | 37% helix, 17% strand | A0A192GPS6 |
Ligands and binding sites
- SAM · S-adenosylmethionine · ligand · 2 copies · chains A, B
- SO4 · Sulfate ion · ion · 4 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 873 | 0.71 | 0.76 | 75 | SAM, SO4 |
| 2 | 791 | 0.69 | 0.76 | 63 | SAM, SO4 |
Interfaces
1 interface between chains.
- A–B · 847 Ų buried · 3 hydrogen bonds · protein-protein
Compared structures
- 5VIM · Crystal structure of the Zika virus NS5 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 A0A192GPS6
- Elsewhere: RCSB PDB 5VIM · PDBe 5VIM · UniProt A0A192GPS6
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