PDBe 2pec

X-ray diffraction
2.2Å resolution

THE REFINED THREE-DIMENSIONAL STRUCTURE OF PECTATE LYASE C FROM ERWINIA CHRYSANTHEMI AT 2.2 ANGSTROMS RESOLUTION: IMPLICATIONS FOR AN ENZYMATIC MECHANISM

Released:
Source organism: Dickeya chrysanthemi
Primary publication:
Protein motifs. 3. The parallel beta helix and other coiled folds.
FASEB J. 9 335-42 (1995)
PMID: 7896002

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: Not provided
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

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
Spacegroup: P212121
Unit cell:
a: 73.38Å b: 80.26Å c: 95.12Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.18 0.18 not available
Expression system: Not provided