6b4p

X-ray diffraction
1.55Å resolution

Crystal Structure of Peptidylprolyl Isomerase from Naegleria fowleri

Released:
Source organism: Naegleria fowleri
Entry author: Seattle Structural Genomics Center for Infectious Disease (SSGCID)

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo dimer
PDBe Complex ID:
PDB-CPX-104231 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
peptidylprolyl isomerase Chains: A, B
Molecule details ›
Chains: A, B
Length: 127 amino acids
Theoretical weight: 14.21 KDa
Source organism: Naegleria fowleri
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A2H4A315 (Residues: 1-119; Coverage: 100%)
Gene names: FDP41_012078, NF0084240
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase
Structure domains: Chitinase A; domain 3

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 21-ID-F
Spacegroup: P21
Unit cell:
a: 37.25Å b: 61.15Å c: 45.76Å
α: 90° β: 90.28° γ: 90°
R-values:
R R work R free
0.157 0.155 0.187
Expression system: Escherichia coli BL21(DE3)