4OB2
Crystal Structure of Nitrile Hydratase from Pseudonocardia thermophila bound to Butaneboronic Acid via Crystal Soaking
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| A | 0005515 | molecular_function | protein binding |
| A | 0005575 | cellular_component | cellular_component |
| A | 0016829 | molecular_function | lyase activity |
| A | 0018822 | molecular_function | nitrile hydratase activity |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0046914 | molecular_function | transition metal ion binding |
| A | 0050897 | molecular_function | cobalt ion binding |
| A | 0050899 | biological_process | nitrile catabolic process |
| A | 0080109 | molecular_function | indole-3-acetonitrile nitrile hydratase activity |
| B | 0005515 | molecular_function | protein binding |
| B | 0005575 | cellular_component | cellular_component |
| B | 0016829 | molecular_function | lyase activity |
| B | 0018822 | molecular_function | nitrile hydratase activity |
| B | 0046914 | molecular_function | transition metal ion binding |
| B | 0050899 | biological_process | nitrile catabolic process |
| B | 0080109 | molecular_function | indole-3-acetonitrile nitrile hydratase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE BUB A 301 |
| Chain | Residue |
| A | CSD111 |
| A | SER112 |
| A | CYS113 |
| A | ARG167 |
| A | CO302 |
| B | ARG52 |
| site_id | AC2 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CO A 302 |
| Chain | Residue |
| A | CYS113 |
| A | BUB301 |
| A | CYS108 |
| A | CSD111 |
| A | SER112 |
| site_id | AC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL A 303 |
| Chain | Residue |
| A | LEU73 |
| A | ALA74 |
| A | MET93 |
| A | MET166 |
| A | HOH431 |
| A | HOH439 |
| A | HOH566 |
| B | LYS171 |
| B | HIS173 |
| site_id | AC4 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 305 |
| Chain | Residue |
| A | TYR46 |
| A | GLU47 |
| A | ASN48 |
| A | VAL50 |
| A | HIS53 |
| A | HOH458 |
| B | VAL24 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL A 306 |
| Chain | Residue |
| A | HIS104 |
| A | LYS158 |
| A | HOH443 |
| A | HOH557 |
| A | HOH629 |
| site_id | AC6 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 307 |
| Chain | Residue |
| A | GLU25 |
| A | ILE39 |
| A | ASP40 |
| A | HOH622 |
| B | GLU28 |
| B | VAL32 |
| B | LEU106 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 301 |
| Chain | Residue |
| B | GLY142 |
| B | THR228 |
| B | HOH696 |
| site_id | AC8 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GOL B 302 |
| Chain | Residue |
| B | MET1 |
| B | GLY3 |
| B | TYR5 |
| B | ASP11 |
| B | GLY12 |
| B | GLU56 |
| B | GLN57 |
| B | LYS153 |
| B | HOH551 |
| B | HOH579 |
| B | HOH639 |
| site_id | AC9 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 303 |
| Chain | Residue |
| B | ARG146 |
| B | PHE147 |
| B | SER148 |
| B | PRO221 |
| B | TYR222 |
| B | ILE223 |
| B | GLU224 |
| B | HOH580 |
| B | HOH615 |
| site_id | BC1 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GOL B 304 |
| Chain | Residue |
| B | GLU50 |
| B | ALA182 |
| B | GLY185 |
| B | LEU186 |
| B | GLY187 |
| B | HOH506 |
| B | HOH522 |
| B | HOH574 |
| B | HOH576 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:11700034 |
| Chain | Residue | Details |
| A | CYS108 | |
| A | CSD111 | |
| A | SER112 | |
| A | CYS113 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: Cysteine sulfinic acid (-SO2H) => ECO:0000269|PubMed:11700034 |
| Chain | Residue | Details |
| A | CSD111 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:11700034 |
| Chain | Residue | Details |
| A | CYS113 |
