› 2afu

X-ray diffraction
2.22Å resolution

Crystal structure of human glutaminyl cyclase in complex with glutamine t-butyl ester

Released:
DOI: 10.2210/pdb2afu/pdb
PDB entry 2afu coloured by chain, front view.
PDB entry 2afu coloured by chain, side view.
PDB entry 2afu coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation.
Huang KF, Liu YL, Cheng WJ, Ko TP, Wang AH
Proc Natl Acad Sci U S A 102 13117-22 (2005)
PMID: 16135565

Function and Biology Details

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

Structure analysis Details

Assemblies composition:
monomeric (preferred)
homo hexamer
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: 37.56 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:
Ligand ZN 2 x ZN
Ligand BGT 2 x BGT
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU, PHOTON FACTORY BEAMLINE BL-5A
Spacegroup: R32
Unit cell:
a: 119.137Å b: 119.137Å c: 332.612Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.198 0.188 0.226
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

9 review citations

Glutaminyl cyclases from animals and plants: a case of functionally convergent protein evolution.
Schilling et al. (2008)
8 more

2 mentions without citation

Crystal structures of human glutaminyl cyclase, an enzyme responsible for protein N-terminal pyroglutamate formation.
Huang et al. (2005)
1 more