3A2Z
E. coli Gsp amidase Cys59 sulfenic acid
Summary for 3A2Z
Entry DOI | 10.2210/pdb3a2z/pdb |
Related | 2iob 3a2y 3a30 |
Descriptor | Bifunctional glutathionylspermidine synthetase/amidase (2 entities in total) |
Functional Keywords | gsp amidase, atp-binding, hydrolase, ligase, multifunctional enzyme, nucleotide-binding |
Biological source | Escherichia coli |
Total number of polymer chains | 1 |
Total formula weight | 22293.91 |
Authors | Pai, C.-H.,Ko, T.-P.,Chiang, B.-Y.,Lin, C.-H.,Wang, A.H.-J. (deposition date: 2009-06-05, release date: 2010-05-19, Last modification date: 2023-11-01) |
Primary citation | Chiang, B.-Y.,Chen, T.-C.,Pai, C.-H.,Chou, C.-C.,Chen, H.-H.,Ko, T.-P.,Hsu, W.-H.,Chang, C.-Y.,Wu, W.-F.,Wang, A.H.-J.,Lin, C.-H. Protein S-thiolation by Glutathionylspermidine (Gsp): the role of Escherichia coli Gsp synthetASE/amidase in redox regulation J.Biol.Chem., 285:25345-25353, 2010 Cited by PubMed: 20530482DOI: 10.1074/jbc.M110.133363 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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