Research workbench
Crystal structure of dengue-2 virus methyltransferase complexed with S-adenosyl-L-homocysteine
Analyse Crystal structure of dengue-2 virus methyltransferase complexed with… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 3EVG
- Type
- protein
- Length
- 257 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA-directed RNA polymerase NS5
- EC
- 2.1.1.56, 2.7.7.48
- UniProt
- P29991
- Ligands
- SAH, SO4
- Pockets
- 1 · best druggability 0.65
Structure
x-ray diffraction · 1 distinct chain · 38% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA-directed RNA polymerase NS5 (EC 2.1.1.56, 2.7.7.48) | protein | 257 | 38% helix, 16% strand | P29991 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
1 pocket found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 482 | 0.65 | 0.78 | 44 | SO4, SAH |
Compared structures
- 3EVG · Crystal structure of Dengue-2 virus methyltransferase complexed with… · 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 P29991
- Elsewhere: RCSB PDB 3EVG · PDBe 3EVG · UniProt P29991
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