MolNFT v1 · #127265 · protein
Structural basis of zika virus methyltransferase inhibition by sinefungin
5MRK: “Structural basis of zika virus methyltransferase inhibition by sinefungin”. X-ray diffraction, 1 ligand (CL). MolNFT v1 #127265 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5MRK
- Type
- protein
- Length
- 507 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- UniProt
- A0A1B0YUR2
- Ligands
- CL
Structure
x-ray diffraction · 2 distinct chains.
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | — | protein | 261 | — | A0A1B0YUR2 |
| B | — | protein | 246 | — | A0A1B0YUR2 |
Ligands and binding sites
- CL · Chloride ion · ion · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Compared structures
- 5MRK · Structural basis of Zika virus methyltransferase inhibition by sinefungin · 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 A0A1B0YUR2
- Elsewhere: RCSB PDB 5MRK · PDBe 5MRK · UniProt A0A1B0YUR2
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