› 3pbe

X-ray diffraction
1.95Å resolution

Crystal structure of the mutant W207F of human secretory glutaminyl cyclase

Released:
DOI: 10.2210/pdb3pbe/pdb
PDB entry 3pbe coloured by chain, front view.
PDB entry 3pbe coloured by chain, side view.
PDB entry 3pbe 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:
Cellular component:
Sequence domains:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo trimer
Assembly name:
PDBe Complex ID:
PDB-CPX-172570 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaminyl-peptide cyclotransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 329 amino acids
Theoretical weight: 37.52 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q16769 (Residues: 33-361; Coverage: 99%)
Gene name: QPCT
Sequence domains: Peptidase family M28
Structure domains: Zn peptidases

Ligands and Environments

2 bound ligands:
Ligand ZN 2 x ZN
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: R32
Unit cell:
a: 118.754Å b: 118.754Å c: 332.093Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.145 0.143 0.19
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)
17 other articles

2 mentions 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)
1 more