5JRO
The crystal structure of azoreductase from Yersinia pestis CO92 in its Apo form
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, NAD(P) 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, 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 | 2 |
| Details | binding site for residue GOL A 301 |
| Chain | Residue |
| A | PHE99 |
| B | PHE163 |
| site_id | AC2 |
| Number of Residues | 2 |
| Details | binding site for residue GOL B 301 |
| Chain | Residue |
| A | ALA189 |
| B | PHE99 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|Ref.4, ECO:0007744|PDB:4ESE |
| Chain | Residue | Details |
| A | SER10 | |
| A | SER16 | |
| A | MET96 | |
| B | SER10 | |
| B | SER16 | |
| B | MET96 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01216 |
| Chain | Residue | Details |
| A | SER140 | |
| B | SER140 |
