3IVZ
Crystal structure of hyperthermophilic nitrilase
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0000257 | molecular_function | nitrilase activity |
A | 0016787 | molecular_function | hydrolase activity |
A | 0080061 | molecular_function | indole-3-acetonitrile nitrilase activity |
B | 0000257 | molecular_function | nitrilase activity |
B | 0016787 | molecular_function | hydrolase activity |
B | 0080061 | molecular_function | indole-3-acetonitrile nitrilase activity |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 6 |
Details | BINDING SITE FOR RESIDUE MG A 263 |
Chain | Residue |
A | MET222 |
A | HOH285 |
A | HOH294 |
A | HOH314 |
A | HOH321 |
A | HOH323 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 2 |
Details | ACT_SITE: Proton acceptor => ECO:0000305|PubMed:21095228 |
Chain | Residue | Details |
A | GLU42 | |
B | GLU42 |
site_id | SWS_FT_FI2 |
Number of Residues | 2 |
Details | ACT_SITE: Proton donor => ECO:0000305|PubMed:21095228 |
Chain | Residue | Details |
A | LYS113 | |
B | LYS113 |
site_id | SWS_FT_FI3 |
Number of Residues | 2 |
Details | ACT_SITE: Nucleophile => ECO:0000255|PROSITE-ProRule:PRU00054, ECO:0000269|PubMed:21095228 |
Chain | Residue | Details |
A | CSX146 | |
B | CSX146 |
site_id | SWS_FT_FI4 |
Number of Residues | 2 |
Details | BINDING: BINDING => ECO:0000255 |
Chain | Residue | Details |
A | VAL173 | |
B | VAL173 |