5H0J : The crystal structure of WT Pedobacter heparinus SMUG2

Creators

Weiguo Cao, Department of Genetics and Biochemistry, Clemson University
Wei Xie, State Key Laboratory for Biocontrol, School of Life Sciences, Sun Yat-Sen University
Panjiao Pang, School of Pharmaceutical Sciences, Sun Yat-Sen University

Description

Experimental Technique/Method:X-RAY DIFFRACTION Resolution:1.8 Classification:LYASE Release Date:2017-01-18 Deposition Date:2016-10-04 Revision Date:2017-03-22 Molecular Weight:28208.39 Macromolecule Type:Protein Residue Count:244 Atom Site Count:1876 DOI:10.2210/pdb5h0j/pdb Abstract: Base deamination is a common type of DNA damage that occurs in all organisms. DNA repair mechanisms are essential to maintain genome integrity, in which the base excision repair (BER) pathway plays a major role in the removal of base damage. In the BER pathway, the uracil DNA glycosylase superfamily is responsible for excising the deaminated bases from DNA and generates apurinic/apyrimidinic (AP) sites. Using bioinformatics tools, we identified a family 3 SMUG1-like DNA glycoyslase from

Publication Date

1-18-2017

Publisher

RCSB-PDB

DOI

10.2210/pdb5h0j/pdb

Document Type

Data Set

Recommended Citation

Cao, Weiguo; Xie, Wei; Pang, Panjiao (2017), "5H0J : The crystal structure of WT Pedobacter heparinus SMUG2", RCSB-PDB, doi: 10.2210/pdb5h0j/pdb

https://doi.org/10.2210/pdb5h0j/pdb

Identifier

5H0J

Embargo Date

1-18-2017