2W1V
Crystal structure of mouse nitrilase-2 at 1.4A resolution
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0005737 | cellular_component | cytoplasm |
A | 0005739 | cellular_component | mitochondrion |
A | 0005813 | cellular_component | centrosome |
A | 0005829 | cellular_component | cytosol |
A | 0006107 | biological_process | oxaloacetate metabolic process |
A | 0006528 | biological_process | asparagine metabolic process |
A | 0006541 | biological_process | glutamine 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 | 0050152 | molecular_function | omega-amidase activity |
A | 0106008 | molecular_function | 2-oxoglutaramate amidase activity |
B | 0005737 | cellular_component | cytoplasm |
B | 0005739 | cellular_component | mitochondrion |
B | 0005813 | cellular_component | centrosome |
B | 0005829 | cellular_component | cytosol |
B | 0006107 | biological_process | oxaloacetate metabolic process |
B | 0006528 | biological_process | asparagine metabolic process |
B | 0006541 | biological_process | glutamine 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 | 0050152 | molecular_function | omega-amidase activity |
B | 0106008 | molecular_function | 2-oxoglutaramate amidase activity |
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 | GLU81 | |
B | GLU81 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000255|PROSITE-ProRule:PRU00054 |
Chain | Residue | Details |
A | LYS150 | |
B | LYS150 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU00054 |
Chain | Residue | Details |
A | CYS191 | |
B | CYS191 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | MOD_RES: Phosphoserine => ECO:0000250|UniProtKB:Q9NQR4 |
Chain | Residue | Details |
A | SER64 | |
B | SER64 |
site_id | SWS_FT_FI5 |
Number of Residues | 2 |
Details | MOD_RES: N6-succinyllysine; alternate => ECO:0007744|PubMed:23806337 |
Chain | Residue | Details |
A | LYS106 | |
B | LYS106 |
site_id | SWS_FT_FI6 |
Number of Residues | 4 |
Details | MOD_RES: N6-succinyllysine => ECO:0007744|PubMed:23806337 |
Chain | Residue | Details |
A | LYS161 | |
A | LYS168 | |
B | LYS161 | |
B | LYS168 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1fo6 |
Chain | Residue | Details |
A | GLU81 | |
A | ASN133 | |
A | ASN218 | |
A | GLU166 | |
A | CYS191 | |
A | LYS150 |
site_id | CSA2 |
Number of Residues | 6 |
Details | Annotated By Reference To The Literature 1fo6 |
Chain | Residue | Details |
B | GLU81 | |
B | ASN133 | |
B | ASN218 | |
B | GLU166 | |
B | CYS191 | |
B | LYS150 |