3vmw

X-ray diffraction
1.9Å resolution

Crystal structure of pectate lyase Bsp165PelA from Bacillus sp. N165 in complex with trigalacturonate

Released:
Source organism: Bacillus sp. N16-5

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:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Amb_all domain-containing protein Chain: A
Molecule details ›
Chain: A
Length: 326 amino acids
Theoretical weight: 35.98 KDa
Source organism: Bacillus sp. N16-5
Expression system: Escherichia coli
UniProt:
  • Canonical: D0VP31 (Residues: 37-362; Coverage: 98%)
Gene name: pelA
Sequence domains: Pectate lyase
Structure domains: Single-stranded right-handed beta-helix, Pectin lyase-like

Ligands and Environments

Carbohydrate polymer : NEW Components: ADA
1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13C1
Spacegroup: P21212
Unit cell:
a: 137.902Å b: 48.174Å c: 52.47Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.157 0.154 0.204
Expression system: Escherichia coli