3ly6 Summary

pdbe.org/3ly6
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Crystal structure of human transglutaminase 2 complex with adenosine 5' Triphosphate

The structure was published by Han, B.G., Cho, J.W., Cho, Y.D., Jeong, K.C., Kim, S.Y., and Lee, B.I., in 2010 in a paper entitled "Crystal structure of human transglutaminase 2 in complex with adenosine triphosphate" (abstract).

This crystal structure was determined using X-ray diffraction at a resolution of 3.14 Å and deposited in 2010.

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

This PDB entry contains multiple copies of the structure of Protein-glutamine gamma-glutamyltransferase 2.

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 Protein-glutamine gamma-glutamyltransferase 2 P21980 (1-687) (TGM2_HUMAN)search Homo sapienssearch 100% 697 97%
B Protein-glutamine gamma-glutamyltransferase 2 P21980 (1-687) (TGM2_HUMAN)search Homo sapienssearch 100% 697 97%
C Protein-glutamine gamma-glutamyltransferase 2 P21980 (1-687) (TGM2_HUMAN)search Homo sapienssearch 100% 697 97%


This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P21980 (1 - 687) Protein-glutamine gamma-glutamyltransferase 2 Homo sapiens

Chain Sequence family (Pfam)
A, B, C (P21980) PF00868: Transglutaminase familysearch, PF00927: Transglutaminase family, C-terminal ig like domainsearch, PF01841: Transglutaminase-like superfamilysearch

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

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