4M0C
The crystal structure of a FMN-dependent NADH-azoreductase from Bacillus anthracis str. Ames Ancestor in complex with FMN.
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| 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 as acceptor |
| A | 0016655 | molecular_function | oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor |
| 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 as acceptor |
| B | 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 | 20 |
| Details | BINDING SITE FOR RESIDUE FMN A 301 |
| Chain | Residue |
| A | HIS10 |
| A | GLU128 |
| A | ALA146 |
| A | SER147 |
| A | GLY148 |
| A | GLY149 |
| A | TYR151 |
| A | THR187 |
| A | GOL303 |
| A | HOH407 |
| A | HOH412 |
| A | SER18 |
| B | TRP62 |
| A | VAL19 |
| A | SER20 |
| A | PRO100 |
| A | LEU101 |
| A | HIS102 |
| A | ASN103 |
| A | PHE104 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 302 |
| Chain | Residue |
| A | HIS26 |
| A | GLU29 |
| B | GLU194 |
| B | HOH431 |
| site_id | AC3 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL A 303 |
| Chain | Residue |
| A | TYR157 |
| A | FMN301 |
| B | SER131 |
| site_id | AC4 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE FMN B 301 |
| Chain | Residue |
| A | ILE54 |
| A | TRP62 |
| B | HIS10 |
| B | SER18 |
| B | VAL19 |
| B | SER20 |
| B | PRO100 |
| B | LEU101 |
| B | HIS102 |
| B | ASN103 |
| B | PHE104 |
| B | ALA146 |
| B | SER147 |
| B | GLY148 |
| B | GLY149 |
| B | TYR151 |
| B | THR187 |
| B | HOH422 |
| B | HOH425 |
| B | HOH430 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 302 |
| Chain | Residue |
| A | GLU204 |
| B | ASP191 |
| B | HOH448 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE ZN B 303 |
| Chain | Residue |
| A | ASP178 |
| B | ASP48 |
| B | HOH449 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE GOL B 304 |
| Chain | Residue |
| A | SER131 |
| B | GLY149 |
| B | TYR157 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 4 |
| Details | Binding site: {"evidences":[{"source":"HAMAP-Rule","id":"MF_01216","evidenceCode":"ECO:0000255"}]} |
| Chain | Residue | Details |
