PDBsum entry 3ly6

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Transferase PDB id
Protein chain
683 a.a. *
ATP ×3
* Residue conservation analysis
PDB id:
Name: Transferase
Title: Crystal structure of human transglutaminase 2 complex with a 5' triphosphate
Structure: Protein-glutamine gamma-glutamyltransferase 2. Chain: a, b, c. Synonym: tgm2, tissue transglutaminase, tgasE C, tgc, tg(c) transglutaminase-2, tgase-h. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: tgm2. Expressed in: escherichia coli. Expression_system_taxid: 562.
3.14Å     R-factor:   0.233     R-free:   0.297
Authors: B.G.Han,B.I.Lee
Key ref: B.G.Han et al. (2010). Crystal structure of human transglutaminase 2 in complex with adenosine triphosphate. Int J Biol Macromol, 47, 190-195. PubMed id: 20450932 DOI: 10.1016/j.ijbiomac.2010.04.023
26-Feb-10     Release date:   18-Aug-10    
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Protein chains
Pfam   ArchSchema ?
P21980  (TGM2_HUMAN) -  Protein-glutamine gamma-glutamyltransferase 2
687 a.a.
683 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 Enzyme reactions 
   Enzyme class: E.C.  - Protein-glutamine gamma-glutamyltransferase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein glutamine + alkylamine = protein N5-alkylglutamine + NH3
Protein glutamine
+ alkylamine
= protein N(5)-alkylglutamine
+ NH(3)
      Cofactor: Calcium
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     plasma membrane   5 terms 
  Biological process     positive regulation of cell adhesion   16 terms 
  Biochemical function     protein binding     7 terms  


DOI no: 10.1016/j.ijbiomac.2010.04.023 Int J Biol Macromol 47:190-195 (2010)
PubMed id: 20450932  
Crystal structure of human transglutaminase 2 in complex with adenosine triphosphate.
B.G.Han, J.W.Cho, Y.D.Cho, K.C.Jeong, S.Y.Kim, B.I.Lee.
Transglutaminase 2 (TG2) is a calcium-dependent multifunctional protein associated with various human diseases. We determined the crystal structure of human TG2 in complex with adenosine triphosphate (ATP). The ATP molecule binds to the previously identified guanosine diphosphate (GDP) binding pocket but has different hydrogen bonds and ion interaction with protein. The four residues Arg476, Arg478, Val479 and Tyr583, all of which are involved in both ATP and GDP binding by hydrogen bonds, might play important roles in the stabilization of TG2 by ATP or GDP. However, Ser482 and Arg580, which are involved in GDP binding, do not form hydrogen bond with ATP. Additionally, we newly discovered an intramolecular disulfide bond between Cys230 and Cys370, which formation might regulate the enzymatic activity of TG2.