Title

5H0K : The crystal structure of WT Pedobacter heparinus SMUG2

Creators

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

Description

Experimental Technique/Method:X-RAY DIFFRACTION Resolution:2.25 Classification:LYASE Release Date:2017-01-18 Deposition Date:2016-10-04 Revision Date:2017-03-22 Molecular Weight:28314.52 Macromolecule Type:Protein Residue Count:244 Atom Site Count:1900 DOI:10.2210/pdb5h0k/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/pdb5h0k/pdb

Document Type

Data Set

Recommended Citation

Pang, Panjiao; Cao, Weiguo; Xie, Wei (2017), "5H0K : The crystal structure of WT Pedobacter heparinus SMUG2", RCSB-PDB, doi: 10.2210/pdb5h0k/pdb

https://doi.org/10.2210/pdb5h0k/pdb

Identifier

5H0K

Embargo Date

1-18-2017