1kv3

X-ray diffraction
2.8Å resolution

HUMAN TISSUE TRANSGLUTAMINASE IN GDP BOUND FORM

Released:

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)
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
PDBe Complex ID:
PDB-CPX-149493 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-glutamine gamma-glutamyltransferase 2 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 687 amino acids
Theoretical weight: 77.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P21980 (Residues: 1-687; Coverage: 100%)
Gene name: TGM2
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 14-BM-D
Spacegroup: P212121
Unit cell:
a: 132.479Å b: 168.797Å c: 238.568Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.233 0.233 0.272
Expression system: Escherichia coli BL21(DE3)