› 1l9x

X-ray diffraction
1.6Å resolution

Structure of gamma-Glutamyl Hydrolase

Released:
DOI: 10.2210/pdb1l9x/pdb
PDB entry 1l9x coloured by chain, front view.
PDB entry 1l9x coloured by chain, side view.
PDB entry 1l9x coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Three-dimensional structure of human gamma -glutamyl hydrolase. A class I glatamine amidotransferase adapted for a complex substate.
Li H, Ryan TJ, Chave KJ, Van Roey P
J Biol Chem 277 24522-9 (2002)
PMID: 11953431

Function and Biology Details

Reaction catalysed: 
Tetrahydropteroyl-(gamma-glutamyl)(n) + (n-1) H(2)O = 5,6,7,8-tetrahydrofolate + (n-1) L-glutamate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-187764 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Gamma-glutamyl hydrolase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 315 amino acids
Theoretical weight: 35.99 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q92820 (Residues: 25-318; Coverage: 100%)
Gene name: GGH
Sequence domains:
Structure domains: Rossmann fold

Ligands and Environments

1 bound ligand:
Ligand BME 6 x BME
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X25
Spacegroup: P212121
Unit cell:
a: 58.763Å b: 156.451Å c: 161.376Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.181 0.181 0.201
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Gamma-glutamyl hydrolase and drug resistance.
Schneider et al. (2006)
14 other articles

7 mentions without citation

Dead-end elimination with perturbations (DEEPer): a provable protein design algorithm with continuous sidechain and backbone flexibility.
Hallen et al. (2013)
6 more