3nl6

X-ray diffraction
2.61Å resolution

The Crystal Structure of Candida glabrata THI6, a Bifunctional Enzyme involved in Thiamin Biosyhthesis of Eukaryotes

Released:

Function and Biology Details

Reactions catalysed:
4-amino-2-methyl-5-diphosphomethylpyrimidine + 2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate = diphosphate + thiamine phosphate + CO(2)
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole 
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo hexamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
TMP-TENI domain-containing protein Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 540 amino acids
Theoretical weight: 58.13 KDa
Source organism: [Candida] glabrata
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q6FV03 (Residues: 1-540; Coverage: 100%)
Gene names: CAGL0E05808g, THI6
Sequence domains:
Structure domains:

Ligands and Environments

3 bound ligands:

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-E
Spacegroup: C2
Unit cell:
a: 163.173Å b: 153.528Å c: 109.618Å
α: 90° β: 117.99° γ: 90°
R-values:
R R work R free
0.223 0.221 0.271
Expression system: Escherichia coli BL21(DE3)