› 5bth

X-ray diffraction
2.2Å resolution

Crystal structure of Candida albicans Rai1

Released:
DOI: 10.2210/pdb5bth/pdb
PDB entry 5bth coloured by chain, front view.
PDB entry 5bth coloured by chain, side view.
PDB entry 5bth coloured by chain, top view.
Source organism: Candida albicans SC5314
Primary publication:
Structural and biochemical studies of the distinct activity profiles of Rai1 enzymes.
Wang VY, Jiao X, Kiledjian M, Tong L
Nucleic Acids Res 43 6596-606 (2015)
PMID: 26101253

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-176866 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Decapping nuclease RAI1 Chain: A
Molecule details ›
Chain: A
Length: 391 amino acids
Theoretical weight: 45.75 KDa
Source organism: Candida albicans SC5314
Expression system: Escherichia coli
UniProt:
  • Canonical: Q5AAT0 (Residues: 1-391; Coverage: 100%)
Gene names: CAALFM_C106800WA, CaO19.13610, CaO19.6230, RAI1
Sequence domains: RAI1 like PD-(D/E)XK nuclease

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: C2221
Unit cell:
a: 85.187Å b: 98.793Å c: 115.557Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.232 0.229 0.292
Expression system: Escherichia coli

Quick links

Citations

5 review citations

New insights into decapping enzymes and selective mRNA decay.
Grudzien-Nogalska et al. (2017)
4 more

1 mention without citation

Structural and biochemical studies of the distinct activity profiles of Rai1 enzymes.
Wang et al. (2015)