› 1nal

X-ray diffraction
2.2Å resolution

THE THREE-DIMENSIONAL STRUCTURE OF N-ACETYLNEURAMINATE LYASE FROM ESCHERICHIA COLI

Released:
DOI: 10.2210/pdb1nal/pdb
PDB entry 1nal coloured by chain, front view.
PDB entry 1nal coloured by chain, side view.
PDB entry 1nal coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
The three-dimensional structure of N-acetylneuraminate lyase from Escherichia coli.
Izard T, Lawrence MC, Malby RL, Lilley GG, Colman PM
Structure 2 361-9 (1994)
PMID: 8081752

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141379 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetylneuraminate lyase Chains: 1, 2, 3, 4
Molecule details ›
Chains: 1, 2, 3, 4
Length: 297 amino acids
Theoretical weight: 32.67 KDa
Source organism: Escherichia coli
UniProt:
  • Canonical: P0A6L4 (Residues: 1-297; Coverage: 100%)
Gene names: JW3194, b3225, nanA, npl
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

1 bound ligand:
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P3221
Unit cell:
a: 122.8Å b: 122.8Å c: 198.8Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.208 0.208 not available

Quick links

Citations

10 review citations

Achievements and challenges of sialic acid research.
Schauer R. (2000)
9 more

20 mentions without citation

Function, structure, and evolution of the RubisCO-like proteins and their RubisCO homologs.
Tabita et al. (2007)
19 more