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 |
| B | 0016829 | molecular_function | lyase activity |
| B | 0018822 | molecular_function | nitrile hydratase activity |
| B | 0046914 | molecular_function | transition metal ion binding |
| C | 0003824 | molecular_function | catalytic activity |
| C | 0016829 | molecular_function | lyase activity |
| C | 0018822 | molecular_function | nitrile hydratase activity |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0046914 | molecular_function | transition metal ion binding |
| D | 0016829 | molecular_function | lyase activity |
| D | 0018822 | molecular_function | nitrile hydratase activity |
| D | 0046914 | molecular_function | transition metal ion binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE A 300 |
| Chain | Residue |
| A | CSD112 |
| A | SER113 |
| A | CSO114 |
| A | NO301 |
| A | CYS109 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 303 |
| Chain | Residue |
| B | HIS29 |
| C | HIS6 |
| C | HOH394 |
| D | GLU31 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE FE C 300 |
| Chain | Residue |
| C | CYS109 |
| C | CSD112 |
| C | SER113 |
| C | CSO114 |
| C | NO301 |
| site_id | AC4 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ZN A 303 |
| Chain | Residue |
| A | HIS6 |
| A | HOH387 |
| A | HOH460 |
| B | GLU31 |
| D | HIS29 |
| site_id | AC5 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 D 304 |
| Chain | Residue |
| B | ARG107 |
| D | GLY14 |
| D | LYS15 |
| D | HOH461 |
| D | HOH462 |
| D | HOH486 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE SO4 A 305 |
| Chain | Residue |
| A | SER182 |
| A | GLN183 |
| D | ARG128 |
| D | THR152 |
| D | HOH309 |
| D | HOH414 |
| site_id | AC7 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE SO4 B 306 |
| Chain | Residue |
| B | GLY14 |
| B | LYS15 |
| B | HOH410 |
| D | ARG107 |
| site_id | AC8 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NO A 301 |
| Chain | Residue |
| A | CSD112 |
| A | SER113 |
| A | CSO114 |
| A | FE300 |
| B | DIO302 |
| site_id | AC9 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE DIO B 302 |
| Chain | Residue |
| A | TRP117 |
| A | NO301 |
| B | TYR37 |
| B | VAL52 |
| B | ARG56 |
| B | TYR76 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE NO C 301 |
| Chain | Residue |
| C | CSD112 |
| C | SER113 |
| C | CSO114 |
| C | FE300 |
| D | DIO302 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE DIO D 302 |
| Chain | Residue |
| C | NO301 |
| D | TYR37 |
| D | VAL52 |
| D | TYR76 |
| site_id | CTA |
| Number of Residues | 4 |
| Details | NON-HEME IRON CENTER AND CATALYTIC SITE IN CHAIN A |
| Chain | Residue |
| A | CYS109 |
| A | CSD112 |
| A | SER113 |
| A | CSO114 |
| site_id | CTB |
| Number of Residues | 4 |
| Details | NON-HEME IRON CENTER AND CATALYTIC SITE IN CHAIN C |
| Chain | Residue |
| C | CYS109 |
| C | CSD112 |
| C | SER113 |
| C | CSO114 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"9586994","evidenceCode":"ECO:0000269"},{"source":"PDB","id":"2AHJ","evidenceCode":"ECO:0007744"}]} |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Cysteine sulfinic acid (-SO2H)","evidences":[{"source":"PubMed","id":"9368004","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"9586994","evidenceCode":"ECO:0000269"}]} |
| site_id | SWS_FT_FI3 |
| Number of Residues | 2 |
| Details | Modified residue: {"description":"Cysteine sulfenic acid (-SOH)","evidences":[{"source":"PubMed","id":"9586994","evidenceCode":"ECO:0000269"}]} |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 10354562, 11293544 |
| Chain | Residue | Details |
| D | ARG56 | |
| C | SER113 | |
| C | CSO114 | |
| C | CSD112 | |
| site_id | CSA2 |
| Number of Residues | 4 |
| Details | a catalytic site defined by CSA, PubMed 10354562, 11293544 |
| Chain | Residue | Details |
| A | SER113 | |
| A | CSO114 | |
| A | CSD112 | |
| B | ARG56 | |
| site_id | MCSA1 |
| Number of Residues | 3 |
| Details | M-CSA 57 |
| Chain | Residue | Details |
| B | ARG56 | electrostatic stabiliser, proton acceptor, proton donor |
| B | TYR72 | proton acceptor, proton donor |
| B | TYR76 | increase acidity, increase basicity |
| A | ILE119 | electrofuge, metal ligand, nucleophile, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 3 |
| Details | M-CSA 57 |
| Chain | Residue | Details |
| D | ARG56 | electrostatic stabiliser, proton acceptor, proton donor |
| D | TYR72 | proton acceptor, proton donor |
| D | TYR76 | increase acidity, increase basicity |
| C | ILE119 | electrofuge, metal ligand, nucleophile, proton acceptor, proton donor |
