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6VTV

Crystal structure of PuuD gamma-glutamyl-gamma-aminobutyrate hydrolase from E. coli

Functional Information from GO Data
ChainGOidnamespacecontents
A0006598biological_processpolyamine catabolic process
A0009447biological_processputrescine catabolic process
A0016787molecular_functionhydrolase activity
A0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
A0033969molecular_functiongamma-glutamyl-gamma-aminobutyrate hydrolase activity
B0006598biological_processpolyamine catabolic process
B0009447biological_processputrescine catabolic process
B0016787molecular_functionhydrolase activity
B0016811molecular_functionhydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides
B0033969molecular_functiongamma-glutamyl-gamma-aminobutyrate hydrolase activity
Functional Information from PDB Data
site_idAC1
Number of Residues6
Detailsbinding site for residue MN A 301
ChainResidue
AHIS145
AHIS161
ASER185
AHIS187
AGLU210
AHOH483

site_idAC2
Number of Residues6
Detailsbinding site for residue MN B 301
ChainResidue
BHIS187
BGLU210
BHOH434
BHIS145
BHIS161
BSER185

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues468
DetailsDomain: {"description":"Glutamine amidotransferase type-1","evidences":[{"source":"PROSITE-ProRule","id":"PRU00605","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI2
Number of Residues2
DetailsActive site: {"description":"Nucleophile","evidences":[{"source":"PROSITE-ProRule","id":"PRU00605","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

site_idSWS_FT_FI3
Number of Residues4
DetailsActive site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00605","evidenceCode":"ECO:0000255"}]}
ChainResidueDetails

246704

PDB entries from 2025-12-24

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