MolNFT v1 · #115376 · protein
N-terminal domain of the vesicular stomatitis virus L protein
5CHS · RNA-directed RNA polymerase L: “N-terminal domain of the vesicular stomatitis virus L protein”. X-ray diffraction, 1 ligand (NA), 9 pockets (best druggability 0.79). MolNFT v1 #115376 on GenesisL1: 3D structure, binding sites and…
- PDB
- 5CHS
- Type
- protein
- Length
- 609 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA-directed RNA polymerase L
- EC
- 2.7.7.48, 2.1.1.56, 2.7.7.-
- UniProt
- Q98776
- Ligands
- NA
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 63% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA-directed RNA polymerase L (EC 2.7.7.48, 2.1.1.56, 2.7.7.-) | protein | 294 | 65% helix, 9% strand | Q98776 |
| B | RNA-directed RNA polymerase L (EC 2.7.7.48, 2.1.1.56, 2.7.7.-) | protein | 315 | 61% helix, 9% strand | Q98776 |
Ligands and binding sites
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 4 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 859 | 0.79 | 0.81 | 72 | empty |
| 2 | 454 | 0.77 | 0.85 | 52 | empty |
| 3 | 111 | 0.57 | 0.84 | 26 | empty |
| 4 | 259 | 0.56 | 0.77 | 36 | empty |
| 5 | 103 | 0.45 | 0.79 | 20 | empty |
Interfaces
1 interface between chains.
- A–B · 2321 Ų buried · 13 hydrogen bonds · protein-protein
Modifications
Observed in the structure: 1 disulfide (disulfide).
Compared structures
- 5CHS · N-terminal domain of the vesicular stomatitis virus L protein · 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 Q98776
- Elsewhere: RCSB PDB 5CHS · PDBe 5CHS · UniProt Q98776
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