› 3h4i

X-ray diffraction
1.3Å resolution

Chimeric Glycosyltransferase for the generation of novel natural products

Released:
DOI: 10.2210/pdb3h4i/pdb
PDB entry 3h4i coloured by chain, front view.
PDB entry 3h4i coloured by chain, side view.
PDB entry 3h4i coloured by chain, top view.
Source organisms:
Primary publication:
Chimeric glycosyltransferases for the generation of hybrid glycopeptides.
Truman AW, Dias MV, Wu S, Blundell TL, Huang F, Spencer JB
Chem Biol 16 676-85 (2009)
PMID: 19549605

Function and Biology Details

Reaction catalysed: 
dTDP-beta-L-4-epi-vancosamine + devancoaminyl-vancomycin = dTDP + chloroorienticin B
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-161221 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
GtfA protein; dTDP-epi-vancosaminyltransferase Chain: A
Molecule details ›
Chain: A
Length: 404 amino acids
Theoretical weight: 42.11 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6ZZJ7 (Residues: 1-4, 209-393; Coverage: 48%)
  • Canonical: P96558 (Residues: 5-205; Coverage: 51%)
Gene names: FHX34_1062, gtfA, tcp8
Sequence domains:
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

2 bound ligands:
Ligand U2F 1 x U2F
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE BM16
Spacegroup: C2221
Unit cell:
a: 111.48Å b: 129.83Å c: 67.44Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.17 0.164 0.184
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

15 review citations

Enzymatic methods for glyco(diversification/randomization) of drugs and small molecules.
Gantt et al. (2011)
14 more

1 mention without citation

Biochemical characterization of a glycosyltransferase Gtf3 from Mycobacterium smegmatis: a case study of improved protein solubilization.
Bakli et al. (2020)