PDBe 2ppo

X-ray diffraction
1.29Å resolution

Crystal structure of E60A mutant of FKBP12

Released:
Source organism: Homo sapiens
Primary publication:
Structural coupling between FKBP12 and buried water.
Proteins 74 603-11 (2009)
PMID: 18704951

Function and Biology Details

Reaction catalysed:
Peptidylproline (omega=180) = peptidylproline (omega=0). 
Biochemical function:
Cellular component:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase FKBP1A Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 11.78 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62942 (Residues: 2-108; Coverage: 99%)
Gene names: FKBP1, FKBP12, FKBP1A
Sequence domains: FKBP-type peptidyl-prolyl cis-trans isomerase

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 8.2.2
Spacegroup: P21
Unit cell:
a: 28.793Å b: 62.563Å c: 32.42Å
α: 90° β: 113.7° γ: 90°
R-values:
R R work R free
0.188 0.133 0.182
Expression system: Escherichia coli