1jyl

X-ray diffraction
2.4Å resolution

Catalytic Mechanism of CTP:phosphocholine Cytidylyltransferase from Streptococcus pneumoniae (LicC)

Released:

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-101450 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Nucleotidyl transferase domain-containing protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 254 amino acids
Theoretical weight: 29.71 KDa
Source organism: Streptococcus pneumoniae
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H2UQB5 (Residues: 2-229; Coverage: 100%)
Gene names: SP_1267, licC
Sequence domains: Nucleotidyl transferase
Structure domains: Spore Coat Polysaccharide Biosynthesis Protein SpsA; Chain A

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-BM
Spacegroup: P1
Unit cell:
a: 48.2Å b: 69Å c: 81.6Å
α: 93.4° β: 92.8° γ: 97.1°
R-values:
R R work R free
0.208 0.208 0.239
Expression system: Escherichia coli