2iaf

X-ray diffraction
2.05Å resolution

Crystal structure of a fragment (residues 11 to 161) of L-serine dehydratase from Legionella pneumophila

Released:
Source organism: Legionella pneumophila
Entry authors: Nocek B, Mulligan R, Moy S, Joachimiak A, Midwest Center for Structural Genomics (MCSG)

Function and Biology Details

Reaction catalysed:
(1a) L-serine = 2-aminoprop-2-enoate + H(2)O
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-178486 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
L-serine dehydratase Chain: A
Molecule details ›
Chain: A
Length: 151 amino acids
Theoretical weight: 16.77 KDa
Source organism: Legionella pneumophila
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q5WYB1 (Residues: 11-161; Coverage: 33%)
Gene names: lpl0828, sdhL
Sequence domains: Serine dehydratase beta chain
Structure domains: D-3-phosphoglycerate dehydrogenase; domain 3

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I212121
Unit cell:
a: 56.319Å b: 76.835Å c: 108.135Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.195 0.224
Expression system: Escherichia coli BL21(DE3)