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PDBsum entry 3pv8

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protein dna_rna ligands metals Protein-protein interface(s) links
Transferase/DNA PDB id
3pv8

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
579 a.a.
DNA/RNA
Ligands
D3T ×2
SO4 ×3
Metals
_MG ×2
Waters ×1823
PDB id:
3pv8
Name: Transferase/DNA
Title: Crystal structure of bacillus DNA polymerase i large fragment bound to DNA and ddttp-da in closed conformation
Structure: DNA polymerase i. Chain: a, d. Fragment: bacillus fragment (analogous to e. Coli klenow fragment). Engineered: yes. Mutation: yes. DNA (5'-d( Cp Cp Tp Gp Ap Cp Tp Cp (2Dt))-3'). Chain: b, e. Fragment: DNA primer strand. Engineered: yes.
Source: Geobacillus kaustophilus. Organism_taxid: 1462. Gene: pola, gk2730. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Synthetic: yes
Resolution:
1.52Å     R-factor:   0.187     R-free:   0.211
Authors: W.Wang,L.S.Beese
Key ref: W.Wang et al. (2011). Structural evidence for the rare tautomer hypothesis of spontaneous mutagenesis. Proc Natl Acad Sci U S A, 108, 17644-17648. PubMed id: 22006298
Date:
06-Dec-10     Release date:   19-Oct-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q5KWC1  (Q5KWC1_GEOKA) -  DNA polymerase I from Geobacillus kaustophilus (strain HTA426)
Seq:
Struc:
 
Seq:
Struc:
878 a.a.
579 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

DNA/RNA chains
  C-C-T-G-A-C-T-C-2DT 9 bases
  A-T-A-A-G-A-G-T-C-A-G-G 12 bases
  C-C-T-G-A-C-T-C-2DT 9 bases
  A-T-A-A-G-A-G-T-C-A-G-G 12 bases

 Enzyme reactions 
   Enzyme class: E.C.2.7.7.7  - DNA-directed Dna polymerase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: DNA(n) + a 2'-deoxyribonucleoside 5'-triphosphate = DNA(n+1) + diphosphate
DNA(n)
+ 2'-deoxyribonucleoside 5'-triphosphate
= DNA(n+1)
+ diphosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
Proc Natl Acad Sci U S A 108:17644-17648 (2011)
PubMed id: 22006298  
 
 
Structural evidence for the rare tautomer hypothesis of spontaneous mutagenesis.
W.Wang, H.W.Hellinga, L.S.Beese.
 
  ABSTRACT  
 
No abstract given.

 

 

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