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
Biochemical function:
Biological process:
Cellular component:
- not assigned
Structure analysis Details
Assembly composition:
hetero dimer (preferred)
Assembly name:
Glutathione hydrolase small chain (preferred)
PDBe Complex ID:
PDB-CPX-157021 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutathione hydrolase large chain
Molecule details ›
Chains: A, C
Length: 376 amino acids
Theoretical weight: 41.45 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Gamma-glutamyltranspeptidase
Structure domains: Serum Albumin; Chain A, Domain 1
Length: 376 amino acids
Theoretical weight: 41.45 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical:
P54422 (Residues: 28-402; Coverage: 67%)
Sequence domains: Gamma-glutamyltranspeptidase
Structure domains: Serum Albumin; Chain A, Domain 1
Glutathione hydrolase small chain
Molecule details ›
Chains: B, D
Length: 193 amino acids
Theoretical weight: 21.1 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
Sequence domains: Gamma-glutamyltranspeptidase
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Length: 193 amino acids
Theoretical weight: 21.1 KDa
Source organism: Bacillus subtilis
Expression system: Escherichia coli BL21(DE3)
UniProt:
- Canonical: P54422 (Residues: 403-587; Coverage: 33%)
Sequence domains: Gamma-glutamyltranspeptidase
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Ligands and Environments
No bound ligands
No modified residues
Experiments and Validation Details
X-ray source:
ESRF BEAMLINE ID14-1
Spacegroup:
P212121
Expression system: Escherichia coli BL21(DE3)
