› 1f74

X-ray diffraction
1.6Å resolution

CRYSTAL STRUCTURE ANALYSIS OF N-ACETYLNEURAMINATE LYASE FROM HAEMOPHILUS INFLUENZAE: CRYSTAL FORM II COMPLEXED WITH 4-DEOXY-SIALIC ACID

Released:
DOI: 10.2210/pdb1f74/pdb
PDB entry 1f74 coloured by chain, front view.
PDB entry 1f74 coloured by chain, side view.
PDB entry 1f74 coloured by chain, top view.
Source organism: Haemophilus influenzae
Primary publication:
Active site modulation in the N-acetylneuraminate lyase sub-family as revealed by the structure of the inhibitor-complexed Haemophilus influenzae enzyme.
Barbosa JA, Smith BJ, DeGori R, Ooi HC, Marcuccio SM, Campi EM, Jackson WR, Brossmer R, Sommer M, Lawrence MC
J Mol Biol 303 405-21 (2000)
PMID: 11031117

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-155184 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
N-acetylneuraminate lyase Chains: A, C
Molecule details ›
Chains: A, C
Length: 293 amino acids
Theoretical weight: 32.56 KDa
Source organism: Haemophilus influenzae
Expression system: Escherichia coli
UniProt:
  • Canonical: P44539 (Residues: 1-293; Coverage: 100%)
Gene names: HI_0142, nanA
Sequence domains: Dihydrodipicolinate synthetase family
Structure domains: Aldolase class I

Ligands and Environments

3 bound ligands:
Ligand NAY 2 x NAY
Ligand GOL 4 x GOL
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MACSCIENCE
Spacegroup: P21212
Unit cell:
a: 65.213Å b: 118.009Å c: 80.968Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.169 0.169 0.202
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Biocatalytic synthesis of hydroxylated natural products using aldolases and related enzymes.
Fessner et al. (2001)
3 more

3 mentions without citation

Interaction preferences across protein-protein interfaces of obligatory and non-obligatory components are different.
De et al. (2005)
2 more