› 6kzb

X-ray diffraction
3.55Å resolution

Function and Biology Details

Reactions catalysed: 
A protein-L-glutamine + a protein-L-lysine = a protein with an N(6)-(gamma-glutamyl)-L-lysine cross-link + NH(3)
Protein L-glutamine + H(2)O = protein L-glutamate + NH(3)
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149493 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-glutamine gamma-glutamyltransferase 2 Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 687 amino acids
Theoretical weight: 77.41 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P21980 (Residues: 1-687; Coverage: 100%)
Gene name: TGM2
Sequence domains:

Ligands and Environments

2 bound ligands:
Ligand CA 6 x CA
Ligand GDP 3 x GDP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: C2221
Unit cell:
a: 133.08Å b: 216.307Å c: 166.263Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.228 0.227 0.262
Expression system: Escherichia coli

Quick links

Citations

1 review citation

Structures of Human Transglutaminase 2: Finding Clues for Interference in Cross-linking Mediated Activity.
Kim et al. (2020)
3 other articles

2 mentions without citation

Competitive Binding of Magnesium to Calcium Binding Sites Reciprocally Regulates Transamidase and GTP Hydrolysis Activity of Transglutaminase 2.
Jeong et al. (2020)
1 more