1o8g

X-ray diffraction
2.2Å resolution

Pectate Lyase C from Erwinia Chrysanthemi at pH 9.5 with 5mM Ca2+

Released:
Source organism: Dickeya chrysanthemi
Primary publication:
Characterization and implications of Ca2+ binding to pectate lyase C.
J. Biol. Chem. 278 12271-7 (2003)
PMID: 12540845

Function and Biology Details

Reaction catalysed:
Eliminative cleavage of (1->4)-alpha-D-galacturonan to give oligosaccharides with 4-deoxy-alpha-D-galact-4-enuronosyl groups at their non-reducing ends
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pectate lyase C Chain: A
Molecule details ›
Chain: A
Length: 353 amino acids
Theoretical weight: 37.73 KDa
Source organism: Dickeya chrysanthemi
Expression system: Escherichia coli
UniProt:
  • Canonical: P11073 (Residues: 23-375; Coverage: 100%)
Gene name: pelC
Sequence domains: Pectate lyase
Structure domains: Single-stranded right-handed beta-helix, Pectin lyase-like

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RT3000
Spacegroup: P212121
Unit cell:
a: 73.18Å b: 81.06Å c: 94.93Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.176 0.176 0.216
Expression system: Escherichia coli