› 6ewr

X-ray diffraction
2.4Å resolution

Putative sugar aminotransferase Spr1654 from Streptococcus pneumoniae, PMP-form

Released:
DOI: 10.2210/pdb6ewr/pdb
PDB 6ewr coloured by chain and viewed from the front.
PDB 6ewr coloured by chain and viewed from the side.
PDB 6ewr coloured by chain and viewed from the top.
Source organism: Streptococcus pneumoniae TIGR4
Primary publication:
Structural and functional studies of Spr1654: an essential aminotransferase in teichoic acid biosynthesis in Streptococcus pneumoniae.
Han X, Sun R, Sandalova T, Achour A
OpenAccess logo Open Biol 8 (2018)
PMID: 29669826

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative capsular polysaccharide biosynthesis protein Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 427 amino acids
Theoretical weight: 47.82 KDa
Source organism: Streptococcus pneumoniae TIGR4
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0H2URM1 (Residues: 1-408; Coverage: 100%)
Gene name: SP_1837
Sequence domains: DegT/DnrJ/EryC1/StrS aminotransferase family

Ligands and Environments

1 bound ligand:
Ligand PMP 4 x PMP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: P21
Unit cell:
a: 78.899Å b: 99.562Å c: 108.095Å
α: 90° β: 97.53° γ: 90°
R-values:
R R work R free
0.245 0.242 0.285
Expression system: Escherichia coli

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Citations

1 citations in other articles

Comparative Proteomic Analysis for a Putative Pyridoxal Phosphate-Dependent Aminotransferase Required for Virulence in Acidovorax citrulli.
Lee et al. (2021)