› 4ntc

X-ray diffraction
1.9Å resolution

Crystal structure of GliT

Released:
DOI: 10.2210/pdb4ntc/pdb
PDB entry 4ntc coloured by chain, front view.
PDB entry 4ntc coloured by chain, side view.
PDB entry 4ntc coloured by chain, top view.
Source organism: Aspergillus fumigatus
Primary publication:
Flavoenzyme-catalyzed formation of disulfide bonds in natural products.
Scharf DH, Groll M, Habel A, Heinekamp T, Hertweck C, Brakhage AA, Huber EM
Angew Chem Int Ed Engl 53 2221-4 (2014)
PMID: 24446392

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-123230 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin reductase gliT Chains: A, B
Molecule details ›
Chains: A, B
Length: 335 amino acids
Theoretical weight: 36.13 KDa
Source organism: Aspergillus fumigatus
Expression system: Escherichia coli
UniProt:
  • Canonical: E9RAH5 (Residues: 1-334; Coverage: 100%)
Gene names: AFUA_6G09740, gliT
Sequence domains: Pyridine nucleotide-disulphide oxidoreductase
Structure domains: FAD/NAD(P)-binding domain

Ligands and Environments

1 bound ligand:
Ligand FAD 2 x FAD
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: P21212
Unit cell:
a: 81.79Å b: 118.18Å c: 69.86Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.184 0.223
Expression system: Escherichia coli

Quick links

Citations

4 review citations

Oxidative Cyclization in Natural Product Biosynthesis.
Tang et al. (2017)
3 more

4 mentions without citation

Chemistry and Enzymology of Disulfide Cross-Linking in Proteins.
Fass et al. (2018)
3 more