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 large chain (preferred)
PDBe Complex ID:
PDB-CPX-148481 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Glutathione hydrolase large chain
Molecule details ›
Chains: A, C
Length: 366 amino acids
Theoretical weight: 39.83 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
Sequence domains: Gamma-glutamyltranspeptidase
Structure domains: Serum Albumin; Chain A, Domain 1
Length: 366 amino acids
Theoretical weight: 39.83 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
- Canonical:
P18956 (Residues: 25-390; Coverage: 66%)
Sequence domains: Gamma-glutamyltranspeptidase
Structure domains: Serum Albumin; Chain A, Domain 1
Glutathione hydrolase small chain
Molecule details ›
Chains: B, D
Length: 190 amino acids
Theoretical weight: 20.26 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
Sequence domains: Gamma-glutamyltranspeptidase
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
Length: 190 amino acids
Theoretical weight: 20.26 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
- Canonical: P18956 (Residues: 391-580; Coverage: 34%)
Sequence domains: Gamma-glutamyltranspeptidase
Structure domains: Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1
