3tue

X-ray diffraction
3Å resolution

The structure of tryparedoxin peroxidase I from Leishmania major

Released:

Function and Biology Details

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Thioredoxin domain-containing protein Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 219 amino acids
Theoretical weight: 24.33 KDa
Source organism: Leishmania major
Expression system: Escherichia coli
UniProt:
  • Canonical: Q4QF76 (Residues: 1-199; Coverage: 100%)
Gene names: LMJF_15_1080, PXN3, TRYP3, TSA, TXNPX
Sequence domains:
Structure domains: Glutaredoxin

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2221
Unit cell:
a: 112.977Å b: 212.385Å c: 90.948Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.199 0.197 0.233
Expression system: Escherichia coli