3CJP
Crystal structure of an uncharacterized amidohydrolase CAC3332 from Clostridium acetobutylicum
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016829 | molecular_function | lyase activity |
A | 0016831 | molecular_function | carboxy-lyase activity |
A | 0019748 | biological_process | secondary metabolic process |
A | 0046872 | molecular_function | metal ion binding |
A | 1901360 | biological_process | organic cyclic compound metabolic process |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016829 | molecular_function | lyase activity |
B | 0016831 | molecular_function | carboxy-lyase activity |
B | 0019748 | biological_process | secondary metabolic process |
B | 0046872 | molecular_function | metal ion binding |
B | 1901360 | biological_process | organic cyclic compound metabolic process |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN A 301 |
Chain | Residue |
A | GLU121 |
A | HIS150 |
A | HIS179 |
site_id | AC2 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN A 302 |
Chain | Residue |
A | HIS8 |
A | HIS10 |
A | GLU121 |
A | ASP227 |
site_id | AC3 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE ZN B 301 |
Chain | Residue |
B | HIS179 |
B | GLU121 |
B | HIS150 |
site_id | AC4 |
Number of Residues | 4 |
Details | BINDING SITE FOR RESIDUE ZN B 302 |
Chain | Residue |
B | HIS8 |
B | HIS10 |
B | GLU121 |
B | ASP227 |