PDBe 3vaw

X-ray diffraction
1.55Å resolution

Crystal structure of a smt fusion peptidyl-prolyl cis-trans isomerase with surface mutation v3i 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:
Peptidyl-prolyl cis-trans isomerase; Ubiquitin-like protein SMT3 Chain: A
Molecule details ›
Chain: A
Length: 209 amino acids
Theoretical weight: 23.02 KDa
Source organisms: Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q12306 (Residues: 13-98, 100-100; Coverage: 86%)
  • Canonical: Q3JK38 (Residues: 3-113; Coverage: 98%)
  • nullnull
Gene names: BURPS1710b_A0907, D9719.15, SMT3, YDR510W
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.1
Spacegroup: P21
Unit cell:
a: 30.94Å b: 31.38Å c: 81.26Å
α: 90° β: 95.03° γ: 90°
R-values:
R R work R free
0.166 0.164 0.194
Expression system: Escherichia coli BL21(DE3)