MolNFT v1 · #189063 · protein
Crystal structure of omsk hemorrhagic fever virus NS5 mtase (in complex with sin)
7V1C · Core protein: “Crystal structure of omsk hemorrhagic fever virus NS5 mtase (in complex with sin)”. X-ray diffraction, 1 ligand (SFG), 2 pockets (best druggability 0.67). MolNFT v1 #189063 on GenesisL1: 3D structure, binding sites…
- PDB
- 7V1C
- Type
- protein
- Length
- 260 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Core protein
- EC
- 3.4.21.91, 3.6.1.15, 3.6.4.13
- UniProt
- C4TPE0
- Ligands
- SFG
- Pockets
- 2 · best druggability 0.67
Structure
x-ray diffraction · 1 distinct chain · 39% helix, 18% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Core protein (EC 3.4.21.91, 3.6.1.15, 3.6.4.13) | protein | 260 | 39% helix, 18% strand | C4TPE0 |
Ligands and binding sites
- SFG · Sinefungin · ligand · chains A
- PEG · Di(hydroxyethyl)ether · additive · 2 copies · chains A
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 596 | 0.67 | 0.77 | 55 | GOL, SFG |
| 2 | 74 | 0.31 | 0.74 | 17 | empty |
Compared structures
- 7V1C · Crystal structure of Omsk hemorrhagic fever virus NS5 MTase (in complex with SIN) · 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 C4TPE0
- Elsewhere: RCSB PDB 7V1C · PDBe 7V1C · UniProt C4TPE0
GL1X is a live explorer of the GenesisL1 blockchain. Turn on JavaScript for search, charts and interactive views.