1iu4

X-ray diffraction
2.4Å resolution

Crystal Structure Analysis of the Microbial Transglutaminase

Released:

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)
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-160522 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-glutamine gamma-glutamyltransferase Chains: A, B, C, D
Molecule details ›
Chains: A, B, C, D
Length: 331 amino acids
Theoretical weight: 37.92 KDa
Source organism: Streptomyces mobaraensis
Expression system: Escherichia coli
UniProt:
  • Canonical: P81453 (Residues: 77-407; Coverage: 88%)
Sequence domains: Microbial transglutaminase
Structure domains: Protein-glutamine gamma-glutamyltransferase

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6B
Spacegroup: P21
Unit cell:
a: 78.41Å b: 117.12Å c: 85.74Å
α: 90° β: 112.8° γ: 90°
R-values:
R R work R free
0.205 0.199 0.266
Expression system: Escherichia coli