4G1B
X-ray structure of yeast flavohemoglobin in complex with econazole
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0000166 | molecular_function | nucleotide binding |
| A | 0008941 | molecular_function | nitric oxide dioxygenase NAD(P)H activity |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0019825 | molecular_function | oxygen binding |
| A | 0020037 | molecular_function | heme binding |
| A | 0046210 | biological_process | nitric oxide catabolic process |
| A | 0046872 | molecular_function | metal ion binding |
| A | 0062197 | biological_process | cellular response to chemical stress |
| A | 0071500 | biological_process | cellular response to nitrosative stress |
| A | 0071949 | molecular_function | FAD binding |
| B | 0000166 | molecular_function | nucleotide binding |
| B | 0008941 | molecular_function | nitric oxide dioxygenase NAD(P)H activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0019825 | molecular_function | oxygen binding |
| B | 0020037 | molecular_function | heme binding |
| B | 0046210 | biological_process | nitric oxide catabolic process |
| B | 0046872 | molecular_function | metal ion binding |
| B | 0062197 | biological_process | cellular response to chemical stress |
| B | 0071500 | biological_process | cellular response to nitrosative stress |
| B | 0071949 | molecular_function | FAD binding |
| C | 0000166 | molecular_function | nucleotide binding |
| C | 0008941 | molecular_function | nitric oxide dioxygenase NAD(P)H activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0019825 | molecular_function | oxygen binding |
| C | 0020037 | molecular_function | heme binding |
| C | 0046210 | biological_process | nitric oxide catabolic process |
| C | 0046872 | molecular_function | metal ion binding |
| C | 0062197 | biological_process | cellular response to chemical stress |
| C | 0071500 | biological_process | cellular response to nitrosative stress |
| C | 0071949 | molecular_function | FAD binding |
| D | 0000166 | molecular_function | nucleotide binding |
| D | 0008941 | molecular_function | nitric oxide dioxygenase NAD(P)H activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0019825 | molecular_function | oxygen binding |
| D | 0020037 | molecular_function | heme binding |
| D | 0046210 | biological_process | nitric oxide catabolic process |
| D | 0046872 | molecular_function | metal ion binding |
| D | 0062197 | biological_process | cellular response to chemical stress |
| D | 0071500 | biological_process | cellular response to nitrosative stress |
| D | 0071949 | molecular_function | FAD binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE HEM A 401 |
| Chain | Residue |
| A | ILE42 |
| A | LEU88 |
| A | ILE90 |
| A | TYR95 |
| A | VAL98 |
| A | ILE129 |
| A | PHE133 |
| A | PRO392 |
| A | LYS393 |
| A | MET394 |
| A | ECN403 |
| A | PHE43 |
| A | ASN44 |
| A | ASN47 |
| A | THR60 |
| A | GLN80 |
| A | ILE81 |
| A | LYS84 |
| A | HIS85 |
| site_id | AC2 |
| Number of Residues | 25 |
| Details | BINDING SITE FOR RESIDUE FAD A 402 |
| Chain | Residue |
| A | ASN44 |
| A | THR46 |
| A | VAL50 |
| A | LYS84 |
| A | TYR189 |
| A | ARG207 |
| A | HIS208 |
| A | TYR209 |
| A | SER210 |
| A | ALA223 |
| A | VAL224 |
| A | LYS225 |
| A | GLU227 |
| A | PHE233 |
| A | PRO234 |
| A | GLY236 |
| A | LEU237 |
| A | VAL238 |
| A | SER239 |
| A | VAL282 |
| A | GLU388 |
| A | PRO389 |
| A | PHE390 |
| A | HOH508 |
| A | HOH527 |
| site_id | AC3 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ECN A 403 |
| Chain | Residue |
| A | ILE24 |
| A | PHE28 |
| A | TYR29 |
| A | ALA56 |
| A | LEU57 |
| A | THR60 |
| A | LEU102 |
| A | TYR126 |
| A | ILE129 |
| A | HEM401 |
| site_id | AC4 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM B 401 |
| Chain | Residue |
| B | ILE42 |
| B | PHE43 |
| B | ASN44 |
| B | ASN47 |
| B | GLN80 |
| B | ILE81 |
| B | LYS84 |
| B | HIS85 |
| B | LEU88 |
| B | ILE90 |
| B | TYR95 |
| B | VAL98 |
| B | ILE129 |
| B | PHE133 |
| B | PRO392 |
| B | LYS393 |
| B | ECN403 |
| site_id | AC5 |
| Number of Residues | 21 |
| Details | BINDING SITE FOR RESIDUE FAD B 402 |
| Chain | Residue |
| B | ASN44 |
| B | VAL50 |
| B | LYS84 |
| B | TYR189 |
| B | ARG207 |
| B | HIS208 |
| B | TYR209 |
| B | SER210 |
| B | ALA223 |
| B | VAL224 |
| B | LYS225 |
| B | GLU227 |
| B | PHE233 |
| B | PRO234 |
| B | GLY236 |
| B | LEU237 |
| B | VAL238 |
| B | SER239 |
| B | VAL282 |
| B | PHE390 |
| B | HOH510 |
| site_id | AC6 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE ECN B 403 |
| Chain | Residue |
| B | HEM401 |
| B | ILE24 |
| B | THR25 |
| B | PHE28 |
| B | TYR29 |
| B | THR60 |
| B | VAL61 |
| B | LEU102 |
| site_id | AC7 |
| Number of Residues | 18 |
| Details | BINDING SITE FOR RESIDUE HEM C 401 |
| Chain | Residue |
| C | ILE42 |
| C | PHE43 |
| C | ASN44 |
| C | ASN47 |
| C | GLN80 |
| C | ILE81 |
| C | LYS84 |
| C | HIS85 |
| C | LEU88 |
| C | ILE90 |
| C | TYR95 |
| C | VAL98 |
| C | ILE129 |
| C | PHE133 |
| C | PRO392 |
| C | LYS393 |
| C | MET394 |
| C | ECN403 |
| site_id | AC8 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FAD C 402 |
| Chain | Residue |
| C | ASN44 |
| C | TYR189 |
| C | ARG207 |
| C | HIS208 |
| C | TYR209 |
| C | SER210 |
| C | ALA223 |
| C | VAL224 |
| C | LYS225 |
| C | GLU227 |
| C | PHE233 |
| C | PRO234 |
| C | GLY236 |
| C | LEU237 |
| C | VAL238 |
| C | SER239 |
| C | VAL282 |
| C | PHE390 |
| C | HOH512 |
| site_id | AC9 |
| Number of Residues | 10 |
| Details | BINDING SITE FOR RESIDUE ECN C 403 |
| Chain | Residue |
| C | ILE24 |
| C | THR25 |
| C | PHE28 |
| C | TYR29 |
| C | GLN53 |
| C | LEU57 |
| C | THR60 |
| C | VAL61 |
| C | VAL98 |
| C | HEM401 |
| site_id | BC1 |
| Number of Residues | 17 |
| Details | BINDING SITE FOR RESIDUE HEM D 401 |
| Chain | Residue |
| D | ILE42 |
| D | PHE43 |
| D | ASN44 |
| D | ASN47 |
| D | GLN80 |
| D | ILE81 |
| D | LYS84 |
| D | HIS85 |
| D | LEU88 |
| D | ILE90 |
| D | TYR95 |
| D | VAL98 |
| D | ILE129 |
| D | PRO392 |
| D | LYS393 |
| D | MET394 |
| D | ECN403 |
| site_id | BC2 |
| Number of Residues | 22 |
| Details | BINDING SITE FOR RESIDUE FAD D 402 |
| Chain | Residue |
| D | ASN44 |
| D | THR46 |
| D | VAL50 |
| D | LYS84 |
| D | TYR189 |
| D | ARG207 |
| D | HIS208 |
| D | TYR209 |
| D | SER210 |
| D | ALA223 |
| D | VAL224 |
| D | LYS225 |
| D | GLU227 |
| D | PHE233 |
| D | PRO234 |
| D | GLY236 |
| D | LEU237 |
| D | VAL238 |
| D | SER239 |
| D | VAL282 |
| D | PHE390 |
| D | HOH507 |
| site_id | BC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE ECN D 403 |
| Chain | Residue |
| D | ILE24 |
| D | THR25 |
| D | PHE28 |
| D | TYR29 |
| D | PHE43 |
| D | GLN53 |
| D | THR60 |
| D | VAL61 |
| D | LEU102 |
| D | TYR126 |
| D | ILE129 |
| D | HEM401 |
