› 2afs

X-ray diffraction
2.22Å resolution

Crystal structure of the genetic mutant R54W of human glutaminyl cyclase

Released:
DOI: 10.2210/pdb2afs/pdb
PDB entry 2afs coloured by chain, front view.
PDB entry 2afs coloured by chain, side view.
PDB entry 2afs 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: 37.59 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 SO4 2 x SO4
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: 119.447Å b: 119.447Å c: 333.848Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.199 0.189 0.222
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

Negative regulation of male development in Caenorhabditis elegans by a protein-protein interaction between TRA-2A and FEM-3.
Mehra et al. (1999)
1 more