2q3z Summary


Transglutaminase 2 undergoes large conformational change upon activation

The structure was published by Pinkas, D.M., Strop, P., Brunger, A.T., and Khosla, C., in 2007 in a paper entitled "Transglutaminase 2 undergoes a large conformational change upon activation" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 2.0 Å and deposited in 2007.

The experimental data on which the structure is based was also deposited.

This PDB entry contains a complex of 2 biomacromolecules, namely Transglutaminase 2 and Polypeptide.

It also contains one or more heterogenic compounds (e.g., ligands, co-factors, ions, modified amino acids, etc.); see here for a complete list.

The molecule has more than one probable quaternary state observed. For more details see the quaternary structure page.

The following tables show cross-reference information to other databases (to obtain a list of all PDB entries sharing the same property or classification, click on the magnifying glass icon):

Chain Name UniProt Name of source organism % of UniProt sequence present in the sample Residues in the sample molecules % of residues observed
A Transglutaminase 2 P21980 (1-687) (TGM2_HUMAN)search Homo sapienssearch 100% 687 95%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P21980 (1 - 687) Transglutaminase 2 Homo sapiens

Chain Structural classification (SCOP) Sequence family (Pfam)
A (P21980) Transglutaminase N-terminal domainsearch, Transglutaminase, two C-terminal domainssearch, Transglutaminase coresearch PF00868: Transglutaminase familysearch, PF00927: Transglutaminase family, C-terminal ig like domainsearch, PF01841: Transglutaminase-like superfamilysearch

Chain ID Molecular function (GO) Biological process (GO) Cellular component (GO)
A (P21980) protein bindingsearch protein-glutamine gamma-glutamyltransferase activitysearch protein domain specific bindingsearch metal ion bindingsearch transferase activitysearch GTP bindingsearch transferase activity, transferring acyl groupssearch positive regulation of cytosolic calcium ion concentration involved in phospholipase C-activating G-protein coupled signaling pathwaysearch peptide cross-linkingsearch positive regulation of mitochondrial calcium ion concentrationsearch negative regulation of endoplasmic reticulum calcium ion concentrationsearch isopeptide cross-linking via N6-(L-isoglutamyl)-L-lysinesearch blood vessel remodelingsearch positive regulation of apoptotic processsearch positive regulation of cell adhesionsearch phospholipase C-activating G-protein coupled receptor signaling pathwaysearch apoptotic cell clearancesearch salivary gland cavitationsearch branching involved in salivary gland morphogenesissearch positive regulation of smooth muscle cell proliferationsearch positive regulation of inflammatory responsesearch protein homooligomerizationsearch positive regulation of I-kappaB kinase/NF-kappaB signalingsearch cytoplasmsearch extracellular vesicular exosomesearch mitochondrionsearch focal adhesionsearch plasma membranesearch cytosolsearch

Chain InterPro annotation
A Transglutaminase, N-terminalsearch Transglutaminase-likesearch Transglutaminase, C-terminalsearch Immunoglobulin-like foldsearch Transglutaminase, conserved sitesearch Immunoglobulin E-setsearch Protein-glutamine gamma-glutamyltransferase, eukaryotasearch