3njv

X-ray diffraction
2.4Å resolution

Rhamnogalacturonan lyase from Aspergillus aculeatus K150A substrate complex

Released:

Function and Biology Details

Reaction catalysed:
Endotype eliminative cleavage of L-alpha-rhamnopyranosyl-(1->4)-alpha-D-galactopyranosyluronic acid bonds of rhamnogalacturonan I domains in ramified hairy regions of pectin leaving L-rhamnopyranose at the reducing end and 4-deoxy-4,5-unsaturated D-galactopyranosyluronic acid at the non-reducing end.
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-169388 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Rhamnogalacturonate lyase A Chain: A
Molecule details ›
Chain: A
Length: 508 amino acids
Theoretical weight: 54.19 KDa
Source organism: Aspergillus aculeatus
Expression system: Aspergillus oryzae
UniProt:
  • Canonical: Q00019 (Residues: 20-527; Coverage: 100%)
Gene names: RGL4, rglA
Sequence domains:
Structure domains:

Ligands and Environments

Carbohydrate polymer : NEW Components: GTR, RAM
2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-5
Spacegroup: P43212
Unit cell:
a: 76.974Å b: 76.974Å c: 170.649Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.188 0.185 0.252
Expression system: Aspergillus oryzae