› 9fxg

X-ray diffraction
1.96Å resolution

Crystal structure of double mutant Y115E Y117E human Glutaminyl Cyclase in apo-state

Released:
DOI: 10.2210/pdb9fxg/pdb
PDB entry 9fxg coloured by chain, front view.
PDB entry 9fxg coloured by chain, side view.
PDB entry 9fxg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Metal Ion Binding to Human Glutaminyl Cyclase: A Structural Perspective.
Tassone G, Pozzi C, Mangani S
Int J Mol Sci 25 (2024)
PMID: 39125848

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-172570 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Glutaminyl-peptide cyclotransferase Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 341 amino acids
Theoretical weight: 38.89 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q16769 (Residues: 15-15, 32-361; Coverage: 95%)
  • Best match: Q16769-2 (Residues: 32-312)
Gene name: QPCT
Sequence domains: Peptidase family M28

Ligands and Environments

2 bound ligands:
Ligand EDO 9 x EDO
Ligand SO4 4 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I04
Spacegroup: C2
Unit cell:
a: 86.281Å b: 149.309Å c: 95.711Å
α: 90° β: 96.96° γ: 90°
R-values:
R R work R free
0.21 0.208 0.257
Expression system: Escherichia coli BL21(DE3)

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