X-ray diffraction
1.05Å resolution

1.05 Angstrom crystal structure of an amino acid ABC transporter substrate-binding protein AbpA from Streptococcus pneumoniae Canada MDR_19A bound to L-arginine

Entry authors: Stogios PJ, Kudritska M, Wawrzak Z, Minasov G, Yim V, Savchenko A, Anderson WF, Center for Structural Genomics of Infectious Diseases (CSGID)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Amino acid ABC transporter, periplasmic amino acid-binding protein, putative Chain: A
Molecule details ›
Chain: A
Length: 269 amino acids
Theoretical weight: 29.3 KDa
Source organism: Streptococcus pneumoniae str. Canada MDR_19A
Expression system: Escherichia coli BL21(DE3)
  • Canonical: A0A0H2ZN67 (Residues: 1-268; Coverage: 100%)
Gene name: SPD_0109
Sequence domains: Bacterial extracellular solute-binding proteins, family 3
Structure domains: Periplasmic binding protein-like II

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-G
Spacegroup: P21
Unit cell:
a: 42.682Å b: 55.028Å c: 46.673Å
α: 90° β: 114.09° γ: 90°
R R work R free
0.166 0.166 0.179
Expression system: Escherichia coli BL21(DE3)