PDBe 3uqa

X-ray diffraction
1.55Å resolution

Crystal structure of a SMT fusion Peptidyl-prolyl cis-trans isomerase with surface mutation A54E from Burkholderia pseudomallei complexed with FK506

Released:

Function and Biology Details

Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0). 
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ubiquitin-like protein SMT3; Peptidyl-prolyl cis-trans isomerase Chain: A
Molecule details ›
Chain: A
Length: 209 amino acids
Theoretical weight: 23.06 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q12306 (Residues: 13-98, 100-100; Coverage: 86%)
  • Canonical: Q63J95 (Residues: 3-113; Coverage: 98%)
  • nullnull
Gene names: BPSS1823, D9719.15, SMT3, YDR510W, fbp
Sequence domains:
Structure domains: Phosphatidylinositol 3-kinase Catalytic Subunit; Chain A, domain 1

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: C2
Unit cell:
a: 96.31Å b: 31.28Å c: 74.32Å
α: 90° β: 121.57° γ: 90°
R-values:
R R work R free
0.182 0.182 0.193
Expression system: Escherichia coli BL21(DE3)