› 1fdy

X-ray diffraction
2.45Å resolution

N-ACETYLNEURAMINATE LYASE IN COMPLEX WITH HYDROXYPYRUVATE

Released:
DOI: 10.2210/pdb1fdy/pdb
PDB entry 1fdy coloured by chain, front view.
PDB entry 1fdy coloured by chain, side view.
PDB entry 1fdy coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structure and mechanism of a sub-family of enzymes related to N-acetylneuraminate lyase.
Lawrence MC, Barbosa JA, Smith BJ, Hall NE, Pilling PA, Ooi HC, Marcuccio SM
J Mol Biol 266 381-99 (1997)
PMID: 9047371

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: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 297 amino acids
Theoretical weight: 32.63 KDa
Source organism: Escherichia coli
Expression system: 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 3PY 4 x 3PY
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE M18X
Spacegroup: P3221
Unit cell:
a: 121Å b: 121Å c: 196.82Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.219 0.219 not available
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Enzyme (re)design: lessons from natural evolution and computation.
Gerlt et al. (2009)
2 more

3 mentions without citation

Structural insights into substrate specificity in variants of N-acetylneuraminic Acid lyase produced by directed evolution.
Campeotto et al. (2010)
2 more