PDBe 3iu0

X-ray diffraction
1.9Å resolution

Structural basis for zymogen activation and substrate binding of transglutaminase from Streptomyces mobaraense

Released:
Source organism: Streptomyces mobaraensis
Entry author: Li TT

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:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
monomeric (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-glutamine gamma-glutamyltransferase Chain: A
Molecule details ›
Chain: A
Length: 382 amino acids
Theoretical weight: 43.33 KDa
Source organism: Streptomyces mobaraensis
Expression system: Escherichia coli
UniProt:
  • Canonical: P81453 (Residues: 32-407; Coverage: 100%)
Structure domains: Microbial transglutaminase. Chain: a

Ligands and Environments

No bound ligands

No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P212121
Unit cell:
a: 64.333Å b: 67.123Å c: 83.969Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.213 0.21 0.244
Expression system: Escherichia coli