1y0o

X-ray diffraction
1.89Å resolution

crystal structure of reduced AtFKBP13

Released:
Source organism: Arabidopsis thaliana
Entry authors: Gayathri G, Swaminathan K

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo decamer
PDBe Complex ID:
PDB-CPX-193442 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP13, chloroplastic Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 129 amino acids
Theoretical weight: 13.61 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9SCY2 (Residues: 80-208; Coverage: 62%)
Gene names: At5g45680, FKBP13, FKBP22-1, FKBPK, MRA19.7
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 17-ID
Spacegroup: C2221
Unit cell:
a: 88.898Å b: 125.753Å c: 119.424Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.203 0.203 0.235
Expression system: Escherichia coli