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 | 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 |
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 | 2 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01216 |
Chain | Residue | Details |
A | SER18 | |
B | SER18 |