› 4k1f

X-ray diffraction
2.34Å resolution

Crystal structure of reduced tryparedoxin peroxidase from leishmania major at 2.34 A resolution

Released:
DOI: 10.2210/pdb4k1f/pdb
PDB entry 4k1f coloured by chain, front view.
PDB entry 4k1f coloured by chain, side view.
PDB entry 4k1f coloured by chain, top view.
Source organism: Leishmania major
Primary publication:
Structure-based discovery of the first non-covalent inhibitors of Leishmania major tryparedoxin peroxidase by high throughput docking.
Brindisi M, Brogi S, Relitti N, Vallone A, Butini S, Gemma S, Novellino E, Colotti G, Angiulli G, Di Chiaro F, Fiorillo A, Ilari A, Campiani G
OpenAccess logo Sci Rep 5 9705 (2015)
PMID: 25951439

Function and Biology Details

Reaction catalysed: 
Thioredoxin + ROOH = thioredoxin disulfide + H(2)O + ROH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-175708 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
thioredoxin-dependent peroxiredoxin Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 199 amino acids
Theoretical weight: 22.16 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

4 bound ligands:
Ligand PGE 1 x PGE
Ligand CL 4 x CL
Ligand PEG 4 x PEG
Ligand PE8 1 x PE8
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ELETTRA BEAMLINE 5.2R
Spacegroup: C2221
Unit cell:
a: 111.811Å b: 226.203Å c: 91.719Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.196 0.194 0.247
Expression system: Escherichia coli

Quick links

Citations

3 review citations

Polyamine-trypanothione pathway: an update.
Ilari et al. (2017)
2 more

3 mentions without citation

Structure-based discovery of the first non-covalent inhibitors of Leishmania major tryparedoxin peroxidase by high throughput docking.
Brindisi et al. (2015)
2 more