› 4pyg

X-ray diffraction
2.8Å resolution

Transglutaminase2 complexed with GTP

Released:
DOI: 10.2210/pdb4pyg/pdb
PDB entry 4pyg coloured by chain, front view.
PDB entry 4pyg coloured by chain, side view.
PDB entry 4pyg coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Crystal structure of transglutaminase 2 with GTP complex and amino acid sequence evidence of evolution of GTP binding site.
Jang TH, Lee DS, Choi K, Jeong EM, Kim IG, Kim YW, Chun JN, Jeon JH, Park HH
OpenAccess logo PLoS One 9 e107005 (2014)
PMID: 25192068

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149488 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Protein-glutamine gamma-glutamyltransferase 2 Chains: A, B, E
Molecule details ›
Chains: A, B, E
Length: 695 amino acids
Theoretical weight: 78.48 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P21980 (Residues: 1-687; Coverage: 100%)
Gene name: TGM2
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand GTP 3 x GTP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PAL/PLS BEAMLINE 5C (4A)
Spacegroup: C2221
Unit cell:
a: 133.546Å b: 216.218Å c: 165.183Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.284 0.236 0.319
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Transglutaminase is a tumor cell and cancer stem cell survival factor.
Eckert et al. (2015)
8 more

20 mentions without citation

Biocatalysis by Transglutaminases: A Review of Biotechnological Applications.
Savoca et al. (2018)
19 more