› 4cag

X-ray diffraction
2.5Å resolution

Bacillus licheniformis Rhamnogalacturonan Lyase PL11

Released:
DOI: 10.2210/pdb4cag/pdb
PDB entry 4cag coloured by chain, front view.
PDB entry 4cag coloured by chain, side view.
PDB entry 4cag coloured by chain, top view.
Source organism: Bacillus licheniformis
Primary publication:
Design of thermostable rhamnogalacturonan lyase mutants from Bacillus licheniformis by combination of targeted single point mutations.
Silva IR, Jers C, Otten H, Nyffenegger C, Larsen DM, Derkx PM, Meyer AS, Mikkelsen JD, Larsen S
Appl Microbiol Biotechnol 98 4521-31 (2014)
PMID: 24419797

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.
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-179214 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Putative polysaccharide lyase family 11 protein Chain: A
Molecule details ›
Chain: A
Length: 596 amino acids
Theoretical weight: 65.15 KDa
Source organism: Bacillus licheniformis
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q65KY4 (Residues: 33-622; Coverage: 100%)
Gene names: BL03786, yesW
Sequence domains:
Structure domains: Immunoglobulins

Ligands and Environments

2 bound ligands:
Ligand CA 10 x CA
Ligand GOL 1 x GOL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-2
Spacegroup: P41212
Unit cell:
a: 95.78Å b: 95.78Å c: 155.65Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.162 0.159 0.226
Expression system: Komagataella pastoris

Quick links

Citations

1 review citation

Thermostability engineering of industrial enzymes through structure modification.
Nezhad et al. (2022)
10 other articles

1 mention without citation

cazy_webscraper: local compilation and interrogation of comprehensive CAZyme datasets.
Hobbs et al. (2023)