› 5htg

X-ray diffraction
2.4Å resolution

Structure of apo P1 form of Candida albicans FKBP12

Released:
DOI: 10.2210/pdb5htg/pdb
PDB entry 5htg coloured by chain, front view.
PDB entry 5htg coloured by chain, side view.
PDB entry 5htg coloured by chain, top view.
Source organism: Candida albicans SC5314
Primary publication:
Structures of Pathogenic Fungal FKBP12s Reveal Possible Self-Catalysis Function.
Tonthat NK, Juvvadi PR, Zhang H, Lee SC, Venters R, Spicer L, Steinbach WJ, Heitman J, Schumacher MA
mBio 7 e00492-16 (2016)
PMID: 27118592

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-151302 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
FK506-binding protein 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 122 amino acids
Theoretical weight: 13.06 KDa
Source organism: Candida albicans SC5314
Expression system: Escherichia coli
UniProt:
  • Canonical: P28870 (Residues: 3-124; Coverage: 98%)
Gene names: CAALFM_C702570CA, CaJ7.0299, CaO19.11186, CaO19.13810, CaO19.3702, CaO19.6452, RBP1, RBP11, RBP12, RBP2
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: OTHER
Spacegroup: P1
Unit cell:
a: 35.899Å b: 38.643Å c: 50.429Å
α: 78.56° β: 69.67° γ: 79.31°
R-values:
R R work R free
0.22 0.217 0.254
Expression system: Escherichia coli

Quick links

Citations

6 review citations

Calcineurin in fungal virulence and drug resistance: Prospects for harnessing targeted inhibition of calcineurin for an antifungal therapeutic approach.
Juvvadi et al. (2017)
5 more