Function and Biology Details
Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
Selective cleavage of Tyr-|-Gly bond in picornavirus polyprotein.
NTP + H(2)O = NDP + phosphate
Biochemical function:
Biological process:
- not assigned
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero 135-mer (preferred)
Assembly name:
Echovirus 18 viral protein 3 (preferred)
PDBe Complex ID:
PDB-CPX-186541 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Echovirus 18 capsid protein 1
Molecule details ›
Chains: A, D, G, J, M, P, S, V, Y, b, e, h, k, n, q
Length: 287 amino acids
Theoretical weight: 32.56 KDa
Source organism: Echovirus E18
UniProt:
Length: 287 amino acids
Theoretical weight: 32.56 KDa
Source organism: Echovirus E18
UniProt:
- Canonical:
Q8V635 (Residues: 569-855; Coverage: 13%)
Echovirus 18 capsid protein 2
Molecule details ›
Chains: B, E, H, K, N, Q, T, W, Z, c, f, i, l, o, r
Length: 260 amino acids
Theoretical weight: 28.8 KDa
Source organism: Echovirus E18
UniProt:
Length: 260 amino acids
Theoretical weight: 28.8 KDa
Source organism: Echovirus E18
UniProt:
- Canonical: Q8V635 (Residues: 70-329; Coverage: 12%)
Echovirus 18 capsid protein 3
Molecule details ›
Chains: C, F, I, L, O, R, U, X, a, d, g, j, m, p, s
Length: 239 amino acids
Theoretical weight: 26.14 KDa
Source organism: Echovirus E18
UniProt:
Structure domains: Jelly Rolls
Length: 239 amino acids
Theoretical weight: 26.14 KDa
Source organism: Echovirus E18
UniProt:
- Canonical: Q8V635 (Residues: 330-568; Coverage: 11%)
Structure domains: Jelly Rolls
