PDB Information

PDB2QMC
MethodX-RAY DIFFRACTION
Host OrganismEscherichia coli
Gene SourceHelicobacter pylori
Primary Citation
Characterization of Helicobacter pylori gamma-glutamyltranspeptidase reveals the molecular basis for substrate specificity and a critical role for the tyrosine 433-containing loop in catalysis.
Morrow, A.L., Williams, K., Sand, A., Boanca, G., Barycki, J.J.
Biochemistry
HeaderTransferase
Released2007-07-15
Resolution1.550
CATH Insert Date21 Feb, 2008

PDB Images (11)

PDB Prints

PDB Chains (4)

Chain ID Date inserted into CATH CATH Status
A 21 Feb, 2008 Chopped
B 21 Feb, 2008 Chopped
C 21 Feb, 2008 Chopped
D 21 Feb, 2008 Chopped

CATH Domains (6)

Domain ID Date inserted into CATH Superfamily CATH Status
2qmcA01 26 Oct, 2009 Holding pen
2qmcA02 26 Oct, 2009 1.10.246.130 Assigned
2qmcB00 26 Oct, 2009 3.60.20.40 Assigned
2qmcC01 26 Oct, 2009 Holding pen
2qmcC02 26 Oct, 2009 1.10.246.130 Assigned
2qmcD00 26 Oct, 2009 Holding pen

UniProtKB Entries (4)

Accession Gene ID Taxon Description
O25743 O25743_HELPY Helicobacter pylori 26695 Gamma-glutamyltranspeptidase (Ggt)
O25743 O25743_HELPY Helicobacter pylori 26695 Gamma-glutamyltranspeptidase (Ggt)
O25743 O25743_HELPY Helicobacter pylori 26695 Gamma-glutamyltranspeptidase (Ggt)
O25743 O25743_HELPY Helicobacter pylori 26695 Gamma-glutamyltranspeptidase (Ggt)