› 3wfz

X-ray diffraction
2.6Å resolution

Crystal structure of Galacto-N-Biose/Lacto-N-Biose I Phosphorylase C236Y Mutant

Released:
DOI: 10.2210/pdb3wfz/pdb
PDB entry 3wfz coloured by chain, front view.
PDB entry 3wfz coloured by chain, side view.
PDB entry 3wfz coloured by chain, top view.
Source organism: Bifidobacterium longum subsp. longum JCM 1217
Primary publication:
Directed evolution to enhance thermostability of galacto-N-biose/lacto-N-biose I phosphorylase.
Koyama Y, Hidaka M, Nishimoto M, Kitaoka M
Protein Eng Des Sel 26 755-61 (2013)
PMID: 24065834

Function and Biology Details

Reaction catalysed: 
Beta-D-galactopyranosyl-(1->3)-N-acetyl-D-glucosamine + phosphate = alpha-D-galactopyranose 1-phosphate + N-acetyl-D-glucosamine
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123107 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
1,3-beta-galactosyl-N-acetylhexosamine phosphorylase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 759 amino acids
Theoretical weight: 85.54 KDa
Source organism: Bifidobacterium longum subsp. longum JCM 1217
Expression system: Escherichia coli
UniProt:
  • Canonical: E8MF13 (Residues: 1-751; Coverage: 100%)
Gene names: BLLJ_1623, lnbp, lnpA
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand NDG 4 x NDG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE AR-NW12A
Spacegroup: P1
Unit cell:
a: 68.617Å b: 112.996Å c: 118.934Å
α: 105.48° β: 90.88° γ: 106.73°
R-values:
R R work R free
0.183 0.179 0.249
Expression system: Escherichia coli

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Citations

3 review citations

In vitro engineering of microbial enzymes with multifarious applications: prospects and perspectives.
Joshi et al. (2015)
2 more