2xhn

X-ray diffraction
1.52Å resolution

Rhamnogalacturonan lyase from Aspergillus aculeatus K150A active site mutant

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.
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-169388 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rhamnogalacturonate lyase A Chains: A, B
Molecule details ›
Chains: A, B
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

3 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: MAX II BEAMLINE I911-5
Spacegroup: C2221
Unit cell:
a: 108.934Å b: 108.978Å c: 170.65Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.116 0.113 0.164
Expression system: Aspergillus oryzae