› 3si0

X-ray diffraction
2.1Å resolution

Structure of glycosylated human glutaminyl cyclase

Released:
DOI: 10.2210/pdb3si0/pdb
PDB entry 3si0 coloured by chain, front view.
PDB entry 3si0 coloured by chain, side view.
PDB entry 3si0 coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of glycosylated mammalian glutaminyl cyclases reveal conformational variability near the active center.
Ruiz-Carrillo D, Koch B, Parthier C, Wermann M, Dambe T, Buchholz M, Ludwig HH, Heiser U, Rahfeld JU, Stubbs MT, Schilling S, Demuth HU
Biochemistry 50 6280-8 (2011)
PMID: 21671571

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

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172570 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecules (2 distinct):
Glutaminyl-peptide cyclotransferase Chain: A
Molecule details ›
Chain: A
Length: 330 amino acids
Theoretical weight: 37.87 KDa
Source organism: Homo sapiens
Expression system: Komagataella pastoris
UniProt:
  • Canonical: Q16769 (Residues: 38-361; Coverage: 97%)
Gene name: QPCT
Sequence domains: Peptidase family M28
Structure domains: Zn peptidases

Ligands and Environments

Carbohydrate polymer : NEW Components: NAG
Carbohydrate polymer
3 bound ligands:
Ligand ZN 1 x ZN
Ligand IMD 1 x IMD
Ligand CL 1 x CL
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: BESSY BEAMLINE 14.1
Spacegroup: C2
Unit cell:
a: 82.408Å b: 63.688Å c: 77.159Å
α: 90° β: 105.76° γ: 90°
R-values:
R R work R free
0.207 0.204 0.264
Expression system: Komagataella pastoris

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)
13 other articles

3 mentions without citation

OGlcNAcylation and phosphorylation have opposing structural effects in tau: phosphothreonine induces particular conformational order.
Brister et al. (2014)
2 more