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PDBsum entry 3ty5

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protein ligands Protein-protein interface(s) links
Transferase PDB id
3ty5

 

 

 

 

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Contents
Protein chains
381 a.a.
Ligands
ATP
ADP
PGE
Waters ×213
PDB id:
3ty5
Name: Transferase
Title: Crystal structure of c. Thermocellum pnkp ligase domain in complex with atp
Structure: Polynucleotide 2',3'-cyclic phosphate phosphodiesterase / polynucleotide 5'-hydroxyl-kinase / polynucleotide 3'-phosphatase. Chain: a, b. Fragment: nucleotide ligase. Engineered: yes. Mutation: yes
Source: Clostridium thermocellum. Organism_taxid: 203119. Strain: atcc 27405. Gene: cthe_2768. Expressed in: escherichia coli. Expression_system_taxid: 469008.
Resolution:
2.40Å     R-factor:   0.180     R-free:   0.225
Authors: P.Smith,L.Wang,S.Shuman
Key ref: P.Smith et al. (2012). The adenylyltransferase domain of bacterial Pnkp defines a unique RNA ligase family. Proc Natl Acad Sci U S A, 109, 2296-2301. PubMed id: 22308407
Date:
23-Sep-11     Release date:   25-Jan-12    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
A3DJ38  (A3DJ38_CLOTH) -  Metallophosphoesterase from Acetivibrio thermocellus (strain ATCC 27405 / DSM 1237 / JCM 9322 / NBRC 103400 / NCIMB 10682 / NRRL B-4536 / VPI 7372)
Seq:
Struc:
 
Seq:
Struc:
870 a.a.
381 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: E.C.6.5.1.3  - Rna ligase (ATP).
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + (ribonucleotide)n-3'-hydroxyl + 5'-phospho-(ribonucleotide)m = (ribonucleotide)n+m + AMP + diphosphate
ATP
Bound ligand (Het Group name = ATP)
corresponds exactly
+ (ribonucleotide)n-3'-hydroxyl
+ 5'-phospho-(ribonucleotide)m
= (ribonucleotide)n+m
+ AMP
+ diphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
Proc Natl Acad Sci U S A 109:2296-2301 (2012)
PubMed id: 22308407  
 
 
The adenylyltransferase domain of bacterial Pnkp defines a unique RNA ligase family.
P.Smith, L.K.Wang, P.A.Nair, S.Shuman.
 
  ABSTRACT  
 
No abstract given.

 

 

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