› 4pa5

X-ray diffraction
1.86Å resolution

Function and Biology Details

Reaction catalysed: 
A protein-L-glutamine + a protein-L-lysine = a protein with an N(6)-(gamma-glutamyl)-L-lysine cross-link + NH(3)
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-154177 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-glutamine gamma-glutamyltransferase Chains: A, B
Molecule details ›
Chains: A, B
Length: 260 amino acids
Theoretical weight: 30.07 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P40746 (Residues: 1-245; Coverage: 100%)
Gene names: BSU31270, tgl, yugV, yuxF
Sequence domains: Protein-glutamine gamma-glutamyltransferase

Ligands and Environments

8 bound ligands:
Ligand PGE 2 x PGE
Ligand EDO 1 x EDO
Ligand SO4 2 x SO4
Ligand ZN 1 x ZN
Ligand DHL 1 x DHL
Ligand GOL 1 x GOL
Ligand PG4 1 x PG4
Ligand FLC 1 x FLC
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID14-1
Spacegroup: P41
Unit cell:
a: 98.35Å b: 98.35Å c: 65.814Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.167 0.167 0.213
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

3 review citations

Transglutaminases: part I-origins, sources, and biotechnological characteristics.
Duarte et al. (2020)
2 more