MolNFT v1 · #189791 · protein
Crystal structures of alphavirus nonstructural protein 4 (NSP4) reveal an intrinsically dynamic RNA-dependent RNA polymerase fold
7VW5 · RNA-directed RNA polymerase NSP4: “Crystal structures of alphavirus nonstructural protein 4 (NSP4) reveal an intrinsically dynamic RNA-dependent…”. X-ray diffraction, 1 ligand (MG), 9 pockets (best druggability 0.79). MolNFT v1…
- PDB
- 7VW5
- Type
- protein
- Length
- 930 residues
- Chains
- 2
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- RNA-directed RNA polymerase NSP4
- EC
- 2.7.7.48
- UniProt
- P03317
- Ligands
- MG
- Pockets
- 9 · best druggability 0.79
Structure
x-ray diffraction · 2 distinct chains · 55% helix, 10% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | RNA-directed RNA polymerase NSP4 (EC 2.7.7.48) | protein | 464 | 55% helix, 9% strand | P03317 |
| B | RNA-directed RNA polymerase NSP4 (EC 2.7.7.48) | protein | 466 | 55% helix, 10% strand | P03317 |
Ligands and binding sites
- MG · Magnesium ion · metal · 2 copies · chains A, B
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
9 pockets found on a 1 Å grid, 7 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 867 | 0.79 | 0.82 | 102 | empty |
| 2 | 738 | 0.78 | 0.82 | 74 | empty |
| 3 | 154 | 0.69 | 0.88 | 27 | empty |
| 4 | 144 | 0.62 | 0.86 | 21 | empty |
| 5 | 190 | 0.62 | 0.83 | 37 | empty |
Interfaces
1 interface between chains.
- A–B · 3784 Ų buried · 38 hydrogen bonds · protein-protein
Compared structures
- 7VW5 · Crystal structures of alphavirus nonstructural protein 4 (nsP4) reveal an intrinsically… · 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 P03317
- Elsewhere: RCSB PDB 7VW5 · PDBe 7VW5 · UniProt P03317
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