4aho

X-ray diffraction
2Å resolution

Crystal Structure of N-acetylneuraminic acid lyase from Staphylococcus aureus with the chemical modification thia-lysine at position 165

Released:

Function and Biology Details

Reaction catalysed:
Aceneneuramate = N-acetyl-D-mannosamine + pyruvate
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
PDBe Complex ID:
PDB-CPX-173512 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetylneuraminate lyase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 299 amino acids
Theoretical weight: 33.92 KDa
Source organism: Staphylococcus aureus subsp. aureus NCTC 8325
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q2G160 (Residues: 1-293; Coverage: 100%)
Gene names: SAOUHSC_00295, nanA
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 82.315Å b: 109.719Å c: 131.373Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.198 0.196 0.235
Expression system: Escherichia coli BL21