› 4mhn

X-ray diffraction
1.15Å resolution

Crystal structure of a glutaminyl cyclase from Ixodes scapularis

Released:
DOI: 10.2210/pdb4mhn/pdb
PDB entry 4mhn coloured by chain, front view.
PDB entry 4mhn coloured by chain, side view.
PDB entry 4mhn coloured by chain, top view.
Source organism: Ixodes scapularis
Primary publication:
Structural and functional analyses of a glutaminyl cyclase from Ixodes scapularis reveal metal-independent catalysis and inhibitor binding.
Huang KF, Hsu HL, Karim S, Wang AH
Acta Crystallogr D Biol Crystallogr 70 789-801 (2014)
PMID: 24598748

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-110587 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaminyl-peptide cyclotransferase Chain: A
Molecule details ›
Chain: A
Length: 326 amino acids
Theoretical weight: 37.81 KDa
Source organism: Ixodes scapularis
Expression system: Escherichia coli
UniProt:
  • Canonical: B7QK46 (Residues: 28-353; Coverage: 99%)
Gene names: IscW_ISCW023264, Qptc
Sequence domains: Peptidase family M28
Structure domains: Zn peptidases

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13C1
Spacegroup: P212121
Unit cell:
a: 55.278Å b: 71.379Å c: 80.076Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.163 0.162 0.181
Expression system: Escherichia coli

Quick links

Citations

4 citation in other articles

Inhibition of a Putative Dihydropyrimidinase from Pseudomonas aeruginosa PAO1 by Flavonoids and Substrates of Cyclic Amidohydrolases.
Huang CY. (2015)
3 more

2 mentions without citation

Structural and functional analyses of a glutaminyl cyclase from Ixodes scapularis reveal metal-independent catalysis and inhibitor binding.
Huang et al. (2014)
1 more