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3FNM

Crystal structure of acivicin-inhibited gamma-glutamyltranspeptidase reveals critical roles for its C-terminus in autoprocessing and catalysis

Summary for 3FNM
Entry DOI10.2210/pdb3fnm/pdb
Related2NQO 2QMG
DescriptorGamma-glutamyltranspeptidase (Ggt) Large subunit, Gamma-glutamyltranspeptidase (Ggt) Small subunit, (2S)-AMINO[(5S)-3-CHLORO-4,5-DIHYDROISOXAZOL-5-YL]ACETIC ACID, ... (4 entities in total)
Functional Keywordsntn-hydrolase, glutamyltranspeptidase, transferase
Biological sourceHelicobacter pylori (Campylobacter pylori)
More
Total number of polymer chains4
Total formula weight122332.28
Authors
Williams, K.,Cullati, S.,Sand, A.,Biterova, E.I.,Barycki, J.J. (deposition date: 2008-12-25, release date: 2009-05-19, Last modification date: 2017-11-01)
Primary citationWilliams, K.,Cullati, S.,Sand, A.,Biterova, E.I.,Barycki, J.J.
Crystal Structure of Acivicin-Inhibited gamma-Glutamyltranspeptidase Reveals Critical Roles for Its C-Terminus in Autoprocessing and Catalysis.
Biochemistry, 48:2459-2467, 2009
Cited by
PubMed: 19256527
DOI: 10.1021/bi8014955
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.7 Å)
Structure validation

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