› 1yw5

X-ray diffraction
1.6Å resolution

Peptidyl-prolyl isomerase ESS1 from Candida albicans

Released:
DOI: 10.2210/pdb1yw5/pdb
PDB entry 1yw5 coloured by chain, front view.
PDB entry 1yw5 coloured by chain, side view.
PDB entry 1yw5 coloured by chain, top view.
Source organism: Candida albicans
Primary publication:
The structure of the Candida albicans Ess1 prolyl isomerase reveals a well-ordered linker that restricts domain mobility.
Li Z, Li H, Devasahayam G, Gemmill T, Chaturvedi V, Hanes SD, Van Roey P
Biochemistry 44 6180-9 (2005)
PMID: 15835905

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-176848 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Peptidyl-prolyl cis-trans isomerase Chain: A
Molecule details ›
Chain: A
Length: 177 amino acids
Theoretical weight: 19.88 KDa
Source organism: Candida albicans
Expression system: Escherichia coli
UniProt:
  • Canonical: Q59KZ2 (Residues: 1-177; Coverage: 100%)
Gene names: CAALFM_C104410CA, ESS1, orf19.12663
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P21
Unit cell:
a: 29.84Å b: 59.52Å c: 44.86Å
α: 90° β: 91.04° γ: 90°
R-values:
R R work R free
0.2 0.2 0.242
Expression system: Escherichia coli

Quick links

Citations

16 citation in other articles

Structural and kinetic analysis of prolyl-isomerization/phosphorylation cross-talk in the CTD code.
Zhang et al. (2012)
15 more

8 mentions without citation

The Ess1 prolyl isomerase: traffic cop of the RNA polymerase II transcription cycle.
Hanes SD. (2014)
7 more