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PDBsum entry 3n0u

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protein metals Protein-protein interface(s) links
Hydrolase, lyase PDB id
3n0u
Jmol
Contents
Protein chains
209 a.a.
Metals
_NA ×3
Waters ×677
PDB id:
3n0u
Name: Hydrolase, lyase
Title: Crystal structure of tm1821, the 8-oxoguanine DNA glycosylas thermotoga maritima
Structure: Probable n-glycosylase/DNA lyase. Chain: a, b, c. Synonym: 8-oxoguanine DNA glycosylase, DNA-(apurinic or apy site) lyase, ap lyase. Engineered: yes
Source: Thermotoga maritima. Organism_taxid: 2336. Gene: ogg, tm1821, tm_1821. Expressed in: escherichia coli. Expression_system_taxid: 511693.
Resolution:
1.50Å     R-factor:   0.152     R-free:   0.190
Authors: D.R.Cooper,A.Roy,Z.S.Derewenda,Integrated Center For Structu Function Innovation (Isfi)
Key ref: D.R.Cooper et al. Crystal structure of tm1821, The 8-Oxoguanine DNA glycosylase of thermotoga maritima. To be published, .
Date:
14-May-10     Release date:   06-Apr-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
Q9X2E1  (OGG1_THEMA) -  Probable N-glycosylase/DNA lyase
Seq:
Struc:
207 a.a.
209 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.4.2.99.18  - DNA-(apurinic or apyrimidinic site) lyase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     metabolic process   5 terms 
  Biochemical function     catalytic activity     6 terms