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 |