1ooc

X-ray diffraction
2.94Å resolution

Mutations in the T1.5 loop of pectate lyase A

Released:
Source organism: Dickeya chrysanthemi
Primary publication:
Effect of mutations in the T1.5 loop of pectate lyase A from Erwinia chrysanthemi EC16.
Acta Crystallogr D Biol Crystallogr 59 1339-42 (2003)
PMID: 12832805

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)
Assembly name:
PDBe Complex ID:
PDB-CPX-142944 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Pectate lyase A Chains: A, B
Molecule details ›
Chains: A, B
Length: 361 amino acids
Theoretical weight: 38.74 KDa
Source organism: Dickeya chrysanthemi
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C1A2 (Residues: 33-393; Coverage: 100%)
Gene name: pelA
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
X-ray source: RIGAKU RU200
Spacegroup: P21212
Unit cell:
a: 94.758Å b: 151.205Å c: 50.897Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.219 0.219 0.275
Expression system: Escherichia coli