› 4ah7

X-ray diffraction
2.3Å resolution

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
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: 298 amino acids
Theoretical weight: 33.84 KDa
Source organism: Staphylococcus aureus subsp. aureus NCTC 8325
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q2G160 (Residues: 2-293; Coverage: 100%)
Gene names: SAOUHSC_00295, nanA
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

No bound ligands
1 modified residue:
Ligand KPI 4 x KPI

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 82.29Å b: 109.86Å c: 131.74Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.208 0.205 0.259
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

Chemical Protein Modification through Cysteine.
Gunnoo et al. (2016)
13 other articles

4 mentions without citation

Structural insights into the recovery of aldolase activity in N-acetylneuraminic acid lyase by replacement of the catalytically active lysine with γ-thialysine by using a chemical mutagenesis strategy.
Timms et al. (2013)
3 more