MolNFT v1 · #118648 · protein + RNA
Enterovirus 71 polymerase elongation complex (C1S1 form)
5F8G · Genome polyprotein: “Enterovirus 71 polymerase elongation complex (C1S1 form)”. X-ray diffraction, 1 ligand (ZN), 4 pockets (best druggability 0.80). MolNFT v1 #118648 on GenesisL1: 3D structure, binding sites and pockets in GL1X.
- PDB
- 5F8G
- Type
- protein + RNA
- Length
- 484 residues
- Chains
- 3
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Genome polyprotein; RNA (35-mer); RNA (5'-R(*UP*GP*UP*UP*CP*GP*AP*CP*GP*AP*GP*AP*GP*AP*GP*…
- UniProt
- E5RPG3
- Ligands
- ZN
- Pockets
- 4 · best druggability 0.80
Structure
x-ray diffraction · 3 distinct chains · 42% helix, 16% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Genome polyprotein | protein | 462 | 42% helix, 16% strand | E5RPG3 |
| B | RNA (35-mer) | rna | 12 | — | — |
| C | RNA (5'-R(*UP*GP*UP*UP*CP*GP*AP*CP*GP*AP*GP*AP*GP*AP*GP*A)- 3') | rna | 10 | — | — |
Ligands and binding sites
- ZN · Zinc ion · metal · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
4 pockets found on a 1 Å grid, 2 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 1180 | 0.80 | 0.82 | 84 | empty |
| 2 | 163 | 0.70 | 0.89 | 31 | empty |
| 3 | 55 | 0.49 | 0.86 | 16 | empty |
| 4 | 75 | 0.48 | 0.83 | 19 | empty |
Interfaces
3 interfaces between chains.
- A–B · 1094 Ų buried · 22 hydrogen bonds · protein-nucleic
- A–C · 711 Ų buried · 11 hydrogen bonds · protein-nucleic
- B–C · 485 Ų buried · 47 hydrogen bonds · nucleic-nucleic
Compared structures
- 5F8G · Enterovirus 71 Polymerase Elongation Complex (C1S1 Form) · 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 E5RPG3
- Elsewhere: RCSB PDB 5F8G · PDBe 5F8G · UniProt E5RPG3
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