› 3pb8

X-ray diffraction
1.13Å resolution

Crystal structure of the catalytic domain of human Golgi-resident glutaminyl cyclase in complex with N-acetylhistamine

Released:
DOI: 10.2210/pdb3pb8/pdb
PDB entry 3pb8 coloured by chain, front view.
PDB entry 3pb8 coloured by chain, side view.
PDB entry 3pb8 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of human Golgi-resident glutaminyl cyclase and its complexes with inhibitors reveal a large loop movement upon inhibitor binding.
Huang KF, Liaw SS, Huang WL, Chia CY, Lo YC, Chen YL, Wang AH
J Biol Chem 286 12439-49 (2011)
PMID: 21288892

Function and Biology Details

Reaction catalysed: 
L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH(3)
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-192687 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaminyl-peptide cyclotransferase-like protein Chain: X
Molecule details ›
Chain: X
Length: 330 amino acids
Theoretical weight: 37.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q9NXS2 (Residues: 53-382; Coverage: 86%)
Gene name: QPCTL
Sequence domains: Peptidase family M28
Structure domains: Zn peptidases

Ligands and Environments

2 bound ligands:
Ligand AHN 1 x AHN
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P212121
Unit cell:
a: 53.301Å b: 68.58Å c: 77.439Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.133 0.131 0.161
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Development and evolution of human glutaminyl cyclase inhibitors (QCIs): an alternative promising approach for disease-modifying treatment of Alzheimer's disease.
Chen et al. (2023)
18 other articles

1 mention without citation

Structures of human Golgi-resident glutaminyl cyclase and its complexes with inhibitors reveal a large loop movement upon inhibitor binding.
Huang et al. (2011)