› 5du2

X-ray diffraction
2.7Å resolution

Structural analysis of EspG2 glycosyltransferase

Released:
DOI: 10.2210/pdb5du2/pdb
PDB 5du2 coloured by chain and viewed from the front.
PDB 5du2 coloured by chain and viewed from the side.
PDB 5du2 coloured by chain and viewed from the top.
Source organism: Actinomadura verrucosospora
Entry authors: Michalska K, Elshahawi SI, Bigelow L, Babnigg G, Thorson JS, Phillips Jr GN, Joachimiak A, Midwest Center for Structural Genomics (MCSG), Enzyme Discovery for Natural Product Biosynthesis (NatPro)

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
EspG2 glycosyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 419 amino acids
Theoretical weight: 45.14 KDa
Source organism: Actinomadura verrucosospora
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A0R4I999 (Residues: 1-399; Coverage: 100%)
Gene name: espG2
Sequence domains: UDP-glucoronosyl and UDP-glucosyl transferase
Structure domains: Glycogen Phosphorylase B;

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 19-ID
Spacegroup: I212121
Unit cell:
a: 51.331Å b: 178.381Å c: 189.598Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.202 0.2 0.236
Expression system: Escherichia coli BL21(DE3)

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