› 4ahp

X-ray diffraction
2.1Å 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: 33.77 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

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

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I02
Spacegroup: P212121
Unit cell:
a: 82.53Å b: 109.56Å c: 131.34Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.196 0.248
Expression system: Escherichia coli BL21

Quick links

Citations

1 review citation

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

1 mention 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)