3X26
Crystal structure of Nitrile Hydratase mutant bR56K complexed with Trimethylacetonitrile, photo-activated for 5 min
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003824 | molecular_function | catalytic activity |
| 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 | 0080109 | molecular_function | indole-3-acetonitrile nitrile hydratase activity |
| B | 0016829 | molecular_function | lyase activity |
| B | 0018822 | molecular_function | nitrile hydratase activity |
| B | 0046914 | molecular_function | transition metal ion binding |
| B | 0080109 | molecular_function | indole-3-acetonitrile nitrile hydratase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 301 |
| Chain | Residue |
| A | CYS109 |
| A | CSD112 |
| A | SER113 |
| A | CSO114 |
| A | HOH556 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE MG A 302 |
| Chain | Residue |
| B | HOH476 |
| B | HOH543 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL A 303 |
| Chain | Residue |
| B | GLU31 |
| B | TRP32 |
| A | SER19 |
| A | TRP23 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 304 |
| Chain | Residue |
| A | THR125 |
| A | TRP126 |
| B | HOH474 |
| B | HOH480 |
| B | HOH523 |
| site_id | AC5 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE TAN B 301 |
| Chain | Residue |
| B | TYR37 |
| B | MET40 |
| B | VAL55 |
| B | TYR72 |
| B | TYR76 |
| site_id | AC6 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE MG B 302 |
| Chain | Residue |
| B | HOH408 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 303 |
| Chain | Residue |
| B | GLU134 |
| B | TYR135 |
| B | SER192 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 304 |
| Chain | Residue |
| B | THR121 |
| B | ARG132 |
| B | LEU208 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:9586994, ECO:0007744|PDB:2AHJ |
| Chain | Residue | Details |
| A | CYS109 | |
| A | CSD112 | |
| A | SER113 | |
| A | CSO114 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: Cysteine sulfinic acid (-SO2H) => ECO:0000269|PubMed:9368004, ECO:0000269|PubMed:9586994 |
| Chain | Residue | Details |
| A | CSD112 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: Cysteine sulfenic acid (-SOH) => ECO:0000269|PubMed:9586994 |
| Chain | Residue | Details |
| A | CSO114 |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 57 |
| Chain | Residue | Details |
| B | LYS56 | electrostatic stabiliser, proton acceptor, proton donor |
| B | TYR72 | proton acceptor, proton donor |
| B | TYR76 | increase acidity, increase basicity |
| A | CSO114 | electrofuge, metal ligand, nucleophile, proton acceptor, proton donor |
