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6MG6

Crystal structure of carbon-nitrogen hydrolase from Helicobacter pylori G27

Functional Information from GO Data
ChainGOidnamespacecontents
A0016787molecular_functionhydrolase activity
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0033388biological_processputrescine biosynthetic process from arginine
A0050126molecular_functionN-carbamoylputrescine amidase activity
B0016787molecular_functionhydrolase activity
B0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
B0033388biological_processputrescine biosynthetic process from arginine
B0050126molecular_functionN-carbamoylputrescine amidase activity
C0016787molecular_functionhydrolase activity
C0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
C0033388biological_processputrescine biosynthetic process from arginine
C0050126molecular_functionN-carbamoylputrescine amidase activity
D0016787molecular_functionhydrolase activity
D0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
D0033388biological_processputrescine biosynthetic process from arginine
D0050126molecular_functionN-carbamoylputrescine amidase activity
Functional Information from PDB Data
site_idAC1
Number of Residues7
Detailsbinding site for residue SO4 A 400
ChainResidue
ASER73
AGLN77
AASP106
AHOH503
AHOH596
AHOH599
BASP60

246704

PDB entries from 2025-12-24

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