1ejo

X-ray diffraction
2.3Å resolution

FAB FRAGMENT OF NEUTRALISING MONOCLONAL ANTIBODY 4C4 COMPLEXED WITH G-H LOOP FROM FMDV.

Released:

Function and Biology Details

Reactions catalysed:
Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1)
NTP + H(2)O = NDP + phosphate
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.
Autocatalytically cleaves itself from the polyprotein of the foot-and-mouth disease virus by hydrolysis of a Lys-|-Gly bond, but then cleaves host cell initiation factor eIF-4G at bonds -Gly-|-Arg- and -Lys-|-Arg-.
Biochemical function:
  • not assigned
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Ig kappa chain V-III region PC 3741/TEPC 111 Chain: L
Molecule details ›
Chain: L
Length: 216 amino acids
Theoretical weight: 23.76 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: P01660 (Residues: 1-111; Coverage: 100%)
Sequence domains: Immunoglobulin V-set domain
Structure domains: Immunoglobulins
Igh protein Chain: H
Molecule details ›
Chain: H
Length: 220 amino acids
Theoretical weight: 23.57 KDa
Source organism: Mus musculus
UniProt:
  • Canonical: Q6PF95 (Residues: 22-115, 116-123, 124-234; Coverage: 48%)
Gene name: Igh
Sequence domains:
Structure domains: Immunoglobulins
Capsid protein VP1 Chain: P
Molecule details ›
Chain: P
Length: 15 amino acids
Theoretical weight: 1.63 KDa
Source organism: Foot-and-mouth disease virus C1
Expression system: Not provided
UniProt:
  • Canonical: P15072 (Residues: 859-873; Coverage: 1%)

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P212121
Unit cell:
a: 48.18Å b: 69.328Å c: 146.539Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.248 0.248 0.262
Expression system: Not provided