› 2ppp

X-ray diffraction
0.94Å resolution

Crystal structure of E60Q mutant of FKBP12

Released:
DOI: 10.2210/pdb2ppp/pdb
PDB entry 2ppp coloured by chain, front view.
PDB entry 2ppp coloured by chain, side view.
PDB entry 2ppp coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structural coupling between FKBP12 and buried water.
Szep S, Park S, Boder ET, Van Duyne GD, Saven JG
Proteins 74 603-11 (2009)
PMID: 18704951

Function and Biology Details

Reaction catalysed: 
Peptidylproline (omega=180) = peptidylproline (omega=0)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-158812 (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: 11.84 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
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: ALS BEAMLINE 8.2.2
Spacegroup: P21
Unit cell:
a: 28.602Å b: 62.517Å c: 32.248Å
α: 90° β: 114.14° γ: 90°
R-values:
R R work R free
0.203 0.203 0.22
Expression system: Escherichia coli

Quick links

Citations

1 review citation

The FKBP families of higher plants: Exploring the structures and functions of protein interaction specialists.
Gollan et al. (2012)
26 other articles

5 mentions without citation

Conformational Dynamics in FKBP Domains: Relevance to Molecular Signaling and Drug Design.
LeMaster et al. (2015)
4 more