1F89
Crystal structure of Saccharomyces cerevisiae Nit3, a member of branch 10 of the nitrilase superfamily
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0006107 | biological_process | oxaloacetate metabolic process |
| A | 0006528 | biological_process | asparagine metabolic process |
| A | 0006541 | biological_process | glutamine metabolic process |
| A | 0006807 | biological_process | obsolete nitrogen compound metabolic 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 | 0043605 | biological_process | amide catabolic process |
| A | 0050152 | molecular_function | omega-amidase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005739 | cellular_component | mitochondrion |
| B | 0006107 | biological_process | oxaloacetate metabolic process |
| B | 0006528 | biological_process | asparagine metabolic process |
| B | 0006541 | biological_process | glutamine metabolic process |
| B | 0006807 | biological_process | obsolete nitrogen compound metabolic 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 | 0043605 | biological_process | amide catabolic process |
| B | 0050152 | molecular_function | omega-amidase activity |
Functional Information from PROSITE/UniProt
| site_id | PS01227 |
| Number of Residues | 21 |
| Details | UPF0012 Uncharacterized protein family UPF0012 signature. GvgICYDMrFPelamlsarkG |
| Chain | Residue | Details |
| A | GLY165-GLY185 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton acceptor => ECO:0000255|PROSITE-ProRule:PRU00054 |
| Chain | Residue | Details |
| A | GLU53 | |
| B | GLU353 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU00054 |
| Chain | Residue | Details |
| A | LYS128 | |
| B | LYS428 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU00054 |
| Chain | Residue | Details |
| A | CYS169 | |
| B | CYS469 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 2 |
| Details | MOD_RES: Phosphothreonine => ECO:0007744|PubMed:18407956 |
| Chain | Residue | Details |
| A | THR34 | |
| B | THR334 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1fo6 |
| Chain | Residue | Details |
| A | ASN111 | |
| A | GLU53 | |
| A | CYS169 | |
| A | GLU144 | |
| A | ASN196 | |
| A | LYS128 |
| site_id | CSA2 |
| Number of Residues | 6 |
| Details | Annotated By Reference To The Literature 1fo6 |
| Chain | Residue | Details |
| B | LYS428 | |
| B | GLU353 | |
| B | CYS469 | |
| B | ASN411 | |
| B | GLU444 | |
| B | ASN496 |
