6xpb

X-ray diffraction
1.74Å resolution

Structure of human GGT1 in complex with 2-amino-4-(((1-((carboxymethyl)amino)-1-oxobutan-2-yl)oxy)(phenoxy)phosphoryl)butanoic acid (ACPB) molecule

Released:

Function and Biology Details

Reactions catalysed:
A (5-L-glutamyl)-peptide + an amino acid = a peptide + a 5-L-glutamyl amino acid
A glutathione-S-conjugate + H(2)O = an (L-cysteinylglycine)-S-conjugate + L-glutamate
Leukotriene C(4) + H(2)O = leukotriene D(4) + L-glutamate
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
PDBe Complex ID:
PDB-CPX-148579 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutathione hydrolase 1 heavy chain Chain: A
Molecule details ›
Chain: A
Length: 353 amino acids
Theoretical weight: 38.53 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P19440 (Residues: 28-380; Coverage: 62%)
Gene names: GGT, GGT1
Sequence domains: Gamma-glutamyltranspeptidase
Glutathione hydrolase 1 light chain Chain: B
Molecule details ›
Chain: B
Length: 189 amino acids
Theoretical weight: 20.01 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: P19440 (Residues: 381-569; Coverage: 33%)
Gene names: GGT, GGT1
Sequence domains: Gamma-glutamyltranspeptidase

Ligands and Environments

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: C2221
Unit cell:
a: 106.362Å b: 124.218Å c: 104.232Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.155 0.153 0.189
Expression system: Komagataella pastoris