3iu0 Summary


Structural basis for zymogen activation and substrate binding of transglutaminase from Streptomyces mobaraense

A publication describing this structure is not available. The depositing authors are Li, T.T.search

This crystal structure was determined using X-ray diffraction at a resolution of 1.9 Å and deposited in 2009.

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

The PDB entry contains the structure of Protein-glutamine gamma-glutamyltransferase. This molecule has the UniProt identifier P81453 (TGAS_STRMB)search. The sample contained 382 residues which is 100% of the natural sequence. Out of 382 residues 345 were observed and are deposited in the PDB.

The molecule is most likely monomeric.

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 P81453 (32-407) (TGAS_STRMB)search Streptomyces mobaraensissearch 100% 382 92%

This entry contains 1 unique UniProt protein:

UniProt accession Name Organism PDB
P81453 (32 - 407) Protein-glutamine gamma-glutamyltransferase Streptomyces mobaraensis

Chain Structural classification (CATH) Sequence family (Pfam)
A (P81453) Microbial transglutaminase. Chain: asearch PF09017: Microbial transglutaminasesearch

Chain ID Molecular function (GO) Biological process (GO)
A (P81453) protein-glutamine gamma-glutamyltransferase activitysearch transferase activitysearch transferase activity, transferring acyl groupssearch metabolic processsearch

Chain InterPro annotation
A Microbial transglutaminasesearch