› 1tyt

X-ray diffraction
2.6Å resolution

CRYSTAL AND MOLECULAR STRUCTURE OF CRITHIDIA FASCICULATA TRYPANOTHIONE REDUCTASE AT 2.6 ANGSTROMS RESOLUTION

Released:
DOI: 10.2210/pdb1tyt/pdb
Model geometry
Fit model/data
PDB entry 1tyt coloured by chain, front view.
PDB entry 1tyt coloured by chain, side view.
PDB entry 1tyt coloured by chain, top view.
Source organism: Crithidia fasciculata
Primary publication:
Structure of trypanothione reductase from Crithidia fasciculata at 2.6 A resolution; enzyme-NADP interactions at 2.8 A resolution.
Bailey S, Fairlamb AH, Hunter WN
Acta Crystallogr D Biol Crystallogr 50 139-54 (1994)
PMID: 15299452

Function and Biology Details

Reaction catalysed: 
Trypanothione + NADP(+) = trypanothione disulfide + NADPH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153807 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Trypanothione reductase Chains: A, B
Molecule details ›
Chains: A, B
Length: 487 amino acids
Theoretical weight: 52.86 KDa
Source organism: Crithidia fasciculata
Expression system: Not provided
UniProt:
  • Canonical: P39040 (Residues: 1-487; Coverage: 99%)
Gene name: TPR
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand FAD 2 x FAD
No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
Spacegroup: P41
Unit cell:
a: 128.8Å b: 128.8Å c: 92.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.161 0.161 not available
Expression system: Not provided

Quick links

Citations

2 review citations

Symmetry at the active site of the ribosome: structural and functional implications.
Agmon et al. (2005)
1 more

1 mention without citation

Leishmanicidal Potential of Hardwickiic Acid Isolated From Croton sylvaticus.
Crentsil et al. (2020)