4F0L
Crystal structure of Amidohydrolase from Brucella melitensis
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005829 | cellular_component | cytosol |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
A | 0019239 | molecular_function | deaminase activity |
A | 0046872 | molecular_function | metal ion binding |
B | 0005829 | cellular_component | cytosol |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
B | 0019239 | molecular_function | deaminase activity |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE A 501 |
Chain | Residue |
A | HIS61 |
A | HIS63 |
A | HIS237 |
A | ASP325 |
A | HOH777 |
A | HOH937 |
site_id | AC2 |
Number of Residues | 5 |
Details | BINDING SITE FOR RESIDUE FMT A 502 |
Chain | Residue |
A | LEU353 |
A | HOH823 |
A | ALA310 |
A | PHE313 |
A | PHE320 |
site_id | AC3 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE FE B 501 |
Chain | Residue |
B | HIS61 |
B | HIS63 |
B | HIS237 |
B | ASP325 |
B | HOH687 |
B | HOH769 |
site_id | AC4 |
Number of Residues | 3 |
Details | BINDING SITE FOR RESIDUE FMT B 502 |
Chain | Residue |
B | ALA310 |
B | PHE320 |
B | HOH721 |