› 4rih

X-ray diffraction
2.22Å resolution

Chimeric Glycosyltransferase LanGT2S8Ac, carbasugar substrate complex

Released:
DOI: 10.2210/pdb4rih/pdb
PDB entry 4rih coloured by chain, front view.
PDB entry 4rih coloured by chain, side view.
PDB entry 4rih coloured by chain, top view.
Source organisms:
Primary publication:
Structural characterization of O- and C-glycosylating variants of the landomycin glycosyltransferase LanGT2.
Tam HK, Härle J, Gerhardt S, Rohr J, Wang G, Thorson JS, Bigot A, Lutterbeck M, Seiche W, Breit B, Bechthold A, Einsle O
Angew Chem Int Ed Engl 54 2811-5 (2015)
PMID: 25581707

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-193221 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glycosyl transferase; Glycosyl transferase homolog Chains: A, B
Molecule details ›
Chains: A, B
Length: 379 amino acids
Theoretical weight: 40.45 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9ZGC0 (Residues: 1-50, 64-302, 304-373; Coverage: 96%)
  • Canonical: Q9RPA7 (Residues: 38-50, 293-293; Coverage: 4%)
Gene names: lanGT2, urdGT2
Sequence domains:
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

2 bound ligands:
Ligand 3R2 2 x 3R2
Ligand MG 1 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P1
Unit cell:
a: 52.87Å b: 59.03Å c: 64.28Å
α: 80.08° β: 69.08° γ: 86.45°
R-values:
R R work R free
0.177 0.176 0.212
Expression system: Escherichia coli BL21(DE3)

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Citations

3 review citations

Glycosyltransferases: mechanisms and applications in natural product development.
Liang et al. (2015)
2 more