6VTV
Crystal structure of PuuD gamma-glutamyl-gamma-aminobutyrate hydrolase from E. coli
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0006598 | biological_process | polyamine catabolic process |
| A | 0009447 | biological_process | putrescine catabolic process |
| A | 0016787 | molecular_function | hydrolase activity |
| A | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| A | 0033969 | molecular_function | gamma-glutamyl-gamma-aminobutyrate hydrolase activity |
| B | 0006598 | biological_process | polyamine catabolic process |
| B | 0009447 | biological_process | putrescine catabolic process |
| B | 0016787 | molecular_function | hydrolase activity |
| B | 0016811 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides |
| B | 0033969 | molecular_function | gamma-glutamyl-gamma-aminobutyrate hydrolase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | binding site for residue MN A 301 |
| Chain | Residue |
| A | HIS145 |
| A | HIS161 |
| A | SER185 |
| A | HIS187 |
| A | GLU210 |
| A | HOH483 |
| site_id | AC2 |
| Number of Residues | 6 |
| Details | binding site for residue MN B 301 |
| Chain | Residue |
| B | HIS187 |
| B | GLU210 |
| B | HOH434 |
| B | HIS145 |
| B | HIS161 |
| B | SER185 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU00605 |
| Chain | Residue | Details |
| A | CYS118 | |
| B | CYS118 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 4 |
| Details | ACT_SITE: ACT_SITE => ECO:0000255|PROSITE-ProRule:PRU00605 |
| Chain | Residue | Details |
| A | HIS226 | |
| A | GLU228 | |
| B | HIS226 | |
| B | GLU228 |
