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PDBsum entry 3u8u

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protein metals Protein-protein interface(s) links
Hydrolase, lyase PDB id
3u8u
Jmol
Contents
Protein chain
(+ 0 more) 275 a.a.
Metals
_CL ×4
_MG ×6
Waters ×835
PDB id:
3u8u
Name: Hydrolase, lyase
Title: Crystal structure of human apurinic/apyridinimic endonucleas a new crystal form
Structure: DNA-(apurinic or apyrimidinic site) lyase. Chain: a, b, c, d, e, f. Synonym: apex nuclease, apen, apurinic-apyrimidinic endonuc ap endonuclease 1, ape-1, ref-1, redox factor-1. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Gene: apex1, ape, ape1, apex, apx, hap1, ref1. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.15Å     R-factor:   0.200     R-free:   0.243
Authors: R.Agarwal,M.D.Naidu
Key ref: R.Agarwal and m.d.naidu Crystal structure of human apurinic/apyridinimic endonuclease, Ape1 in a new crystal form. To be published, .
Date:
17-Oct-11     Release date:   26-Oct-11    
PROCHECK
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 Headers
 References

Protein chains
Pfam   ArchSchema ?
P27695  (APEX1_HUMAN) -  DNA-(apurinic or apyrimidinic site) lyase
Seq:
Struc:
318 a.a.
275 a.a.
Key:    PfamA domain  PfamB 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!
  Cellular component     intracellular   12 terms 
  Biological process     cellular response to cAMP   24 terms 
  Biochemical function     protein binding     27 terms