3U7I
The crystal structure of FMN-dependent NADH-azoreductase 1 (GBAA0966) from Bacillus anthracis str. Ames Ancestor
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003674 | molecular_function | molecular_function |
| A | 0005575 | cellular_component | cellular_component |
| A | 0008150 | biological_process | biological_process |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor |
| A | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| B | 0003674 | molecular_function | molecular_function |
| B | 0005575 | cellular_component | cellular_component |
| B | 0008150 | biological_process | biological_process |
| B | 0009055 | molecular_function | electron transfer activity |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor |
| B | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| C | 0003674 | molecular_function | molecular_function |
| C | 0005575 | cellular_component | cellular_component |
| C | 0008150 | biological_process | biological_process |
| C | 0009055 | molecular_function | electron transfer activity |
| C | 0010181 | molecular_function | FMN binding |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor |
| C | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| D | 0003674 | molecular_function | molecular_function |
| D | 0005575 | cellular_component | cellular_component |
| D | 0008150 | biological_process | biological_process |
| D | 0009055 | molecular_function | electron transfer activity |
| D | 0010181 | molecular_function | FMN binding |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016652 | molecular_function | oxidoreductase activity, acting on NAD(P)H, NAD(P) as acceptor |
| D | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE CL A 221 |
| Chain | Residue |
| A | HIS10 |
| A | SER18 |
| A | SER20 |
| A | ALA146 |
| A | GOL223 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 222 |
| Chain | Residue |
| A | HIS164 |
| A | HOH271 |
| A | HOH290 |
| site_id | AC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL A 223 |
| Chain | Residue |
| A | HIS102 |
| A | THR187 |
| A | CL221 |
| A | HOH234 |
| A | HOH330 |
| A | HOH410 |
| A | LEU101 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE GOL A 224 |
| Chain | Residue |
| A | LYS32 |
| A | ILE35 |
| A | GLU39 |
| A | HOH244 |
| A | HOH280 |
| A | HOH396 |
| A | HOH498 |
| D | LYS32 |
| site_id | AC5 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE PEG A 225 |
| Chain | Residue |
| A | TRP156 |
| C | SER131 |
| C | ASN172 |
| C | HOH240 |
| site_id | AC6 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL B 221 |
| Chain | Residue |
| B | HIS10 |
| B | SER18 |
| B | VAL19 |
| B | SER20 |
| B | ALA146 |
| B | GOL224 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 222 |
| Chain | Residue |
| B | HIS164 |
| B | LYS168 |
| site_id | AC8 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE CL B 223 |
| Chain | Residue |
| B | LYS3 |
| B | GLN87 |
| B | GLN88 |
| B | HOH688 |
| C | ASN2 |
| C | HOH251 |
| site_id | AC9 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE GOL B 224 |
| Chain | Residue |
| B | LEU101 |
| B | HIS102 |
| B | GLY148 |
| B | THR187 |
| B | CL221 |
| site_id | BC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL C 221 |
| Chain | Residue |
| C | HIS10 |
| C | VAL19 |
| C | SER20 |
| C | ALA146 |
| site_id | BC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE CL D 221 |
| Chain | Residue |
| D | HIS10 |
| D | VAL19 |
| D | SER20 |
| D | ALA146 |
| site_id | BC3 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE GOL D 222 |
| Chain | Residue |
| D | LEU101 |
| D | HIS102 |
| D | ASN103 |
| D | HOH419 |
| D | HOH751 |
| D | HOH772 |
| D | HOH843 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01216 |
| Chain | Residue | Details |
| A | SER18 | |
| B | SER18 | |
| C | SER18 | |
| D | SER18 |
