2afo

X-ray diffraction
2.35Å resolution

Crystal structure of human glutaminyl cyclase at pH 8.0

Released:

Function and Biology Details

Reaction catalysed:
L-glutaminyl-peptide = 5-oxoprolyl-peptide + NH(3)
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo hexamer
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: 37.56 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
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:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL12B2, PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: R32
Unit cell:
a: 118.988Å b: 118.988Å c: 332.258Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.195 0.185 0.216
Expression system: Escherichia coli BL21(DE3)