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PDBsum entry 3ly6

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protein ligands Protein-protein interface(s) links
Transferase PDB id
3ly6
Jmol
Contents
Protein chain
683 a.a. *
Ligands
ATP ×3
* Residue conservation analysis
PDB id:
3ly6
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.
Resolution:
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
Date:
26-Feb-10     Release date:   18-Aug-10    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
P21980  (TGM2_HUMAN) -  Protein-glutamine gamma-glutamyltransferase 2
Seq:
Struc:
 
Seq:
Struc:
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.2.3.2.13  - 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  

 

 
    reference    
 
 
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.
 
  ABSTRACT  
 
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.