› 4ivf

X-ray diffraction
2.2Å resolution

Crystal structure of glutathione transferase homolog from Lodderomyces elongisporus, target EFI-501753, with two GSH per subunit

Released:
DOI: 10.2210/pdb4ivf/pdb
PDB entry 4ivf coloured by chain, front view.
PDB entry 4ivf coloured by chain, side view.
PDB entry 4ivf coloured by chain, top view.
Source organism: Lodderomyces elongisporus NRRL YB-4239
Entry authors: Vetting MW, Toro R, Bhosle R, Al Obaidi NF, Morisco LL, Wasserman SR, Sojitra S, Washington E, Scott Glenn A, Chowdhury S, Evans B, Hammonds J, Hillerich B, Love J, Seidel RD, Imker HJ, Armstrong RN, Gerlt JA, Almo SC, Enzyme Function Initiative (EFI)

Function and Biology Details

Reaction catalysed: 
RX + glutathione = HX + R-S-glutathione
Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-107557 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
glutathione transferase Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 231 amino acids
Theoretical weight: 26.49 KDa
Source organism: Lodderomyces elongisporus NRRL YB-4239
Expression system: Escherichia coli
UniProt:
  • Canonical: A5E437 (Residues: 1-222; Coverage: 100%)
Gene name: LELG_04376
Sequence domains:
Structure domains:

Ligands and Environments


Cofactor: Ligand GSH 16 x GSH
1 bound ligand:
Ligand CIT 1 x CIT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 31-ID
Spacegroup: P212121
Unit cell:
a: 90.598Å b: 112.476Å c: 194.384Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.159 0.156 0.223
Expression system: Escherichia coli

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