4C5Z
Crystal structure of A. niger ochratoxinase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004180 | molecular_function | carboxypeptidase activity |
A | 0005576 | cellular_component | extracellular region |
A | 0006508 | biological_process | proteolysis |
A | 0008237 | molecular_function | metallopeptidase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
A | 0046872 | molecular_function | metal ion binding |
B | 0004180 | molecular_function | carboxypeptidase activity |
B | 0005576 | cellular_component | extracellular region |
B | 0006508 | biological_process | proteolysis |
B | 0008237 | molecular_function | metallopeptidase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0016810 | molecular_function | hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds |
B | 0046872 | molecular_function | metal ion binding |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 4 |
Details | ACT_SITE: ACT_SITE => ECO:0000250|UniProtKB:A2R2V4 |
Chain | Residue | Details |
A | LYS246 | |
A | ASP378 | |
B | LYS246 | |
B | ASP378 |
site_id | SWS_FT_FI2 |
Number of Residues | 10 |
Details | BINDING: BINDING => ECO:0000250|UniProtKB:A2R2V4 |
Chain | Residue | Details |
A | HIS111 | |
B | HIS307 | |
A | HIS113 | |
A | LYS246 | |
A | HIS287 | |
A | HIS307 | |
B | HIS111 | |
B | HIS113 | |
B | LYS246 | |
B | HIS287 |