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PDBsum entry 3py8

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protein dna_rna ligands metals links
Transferase/DNA PDB id
3py8

 

 

 

 

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JSmol PyMol  
Contents
Protein chain
539 a.a.
DNA/RNA
Ligands
DCT
GOL ×2
Metals
_MN ×5
_MG
Waters ×523
PDB id:
3py8
Name: Transferase/DNA
Title: Crystal structure of a mutant of the large fragment of DNA polymerase i from thermus aquaticus in a closed ternary complex with DNA and ddctp
Structure: DNA polymerase i. Chain: a. Fragment: DNA polymerase i large fragment. Synonym: taq polymerase 1. Engineered: yes. Mutation: yes. DNA (5'-d( Gp Ap Cp Cp Ap Cp Gp Gp Cp Gp Cp (Doc))-3'). Chain: b. Engineered: yes.
Source: Thermus aquaticus. Organism_taxid: 271. Gene: pola, pol1. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Synthetic: yes
Resolution:
1.74Å     R-factor:   0.171     R-free:   0.199
Authors: A.Schnur,A.Marx,W.Welte,K.Diederichs
Key ref: S.Obeid et al. (2011). Learning from directed evolution: Thermus aquaticus DNA polymerase mutants with translesion synthesis activity. Chembiochem, 12, 1574-1580. PubMed id: 21480455
Date:
12-Dec-10     Release date:   15-Jun-11    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P19821  (DPO1_THEAQ) -  DNA polymerase I, thermostable from Thermus aquaticus
Seq:
Struc:
 
Seq:
Struc:
832 a.a.
539 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

DNA/RNA chains
  G-A-C-C-A-C-G-G-C-G-C-DOC 12 bases
  A-G-G-G-C-G-C-C-G-T-G-G-T-C 14 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    
 
 
Chembiochem 12:1574-1580 (2011)
PubMed id: 21480455  
 
 
Learning from directed evolution: Thermus aquaticus DNA polymerase mutants with translesion synthesis activity.
S.Obeid, A.Schnur, C.Gloeckner, N.Blatter, W.Welte, K.Diederichs, A.Marx.
 
  ABSTRACT  
 
No abstract given.

 

 

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