2HPV
Crystal structure of FMN-Dependent azoreductase from Enterococcus faecalis
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 |
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 | 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 | 19 |
Details | BINDING SITE FOR RESIDUE FMN A 1200 |
Chain | Residue |
A | HIS10 |
A | SER148 |
A | GLY150 |
A | GLY151 |
A | TYR153 |
A | ASP184 |
A | HOH1210 |
A | HOH1237 |
A | HOH1245 |
A | HOH1262 |
B | ILE54 |
A | SER17 |
A | ARG18 |
A | SER19 |
A | PRO103 |
A | MSE104 |
A | TRP105 |
A | ASN106 |
A | LEU107 |
site_id | AC2 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE FMN B 1201 |
Chain | Residue |
A | ILE54 |
B | HIS10 |
B | SER17 |
B | ARG18 |
B | SER19 |
B | PRO103 |
B | MSE104 |
B | TRP105 |
B | ASN106 |
B | LEU107 |
B | SER148 |
B | ASN149 |
B | GLY150 |
B | GLY151 |
B | TYR153 |
B | ASP184 |
B | HOH1204 |
B | HOH1217 |
B | HOH1227 |
B | HOH1252 |
site_id | AC3 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE FMN C 1202 |
Chain | Residue |
C | HIS10 |
C | SER17 |
C | ARG18 |
C | SER19 |
C | PRO103 |
C | MSE104 |
C | TRP105 |
C | ASN106 |
C | LEU107 |
C | SER148 |
C | ASN149 |
C | GLY150 |
C | GLY151 |
C | TYR153 |
C | ASP184 |
C | HOH1204 |
C | HOH1219 |
C | HOH1258 |
C | HOH1297 |
D | ILE54 |
site_id | AC4 |
Number of Residues | 17 |
Details | BINDING SITE FOR RESIDUE FMN D 1203 |
Chain | Residue |
D | HIS10 |
D | SER17 |
D | ARG18 |
D | SER19 |
D | PRO103 |
D | MSE104 |
D | TRP105 |
D | ASN106 |
D | LEU107 |
D | SER148 |
D | ASN149 |
D | GLY150 |
D | GLY151 |
D | TYR153 |
D | ASP184 |
D | HOH1223 |
D | HOH1271 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 12 |
Details | BINDING: BINDING => ECO:0000269|Ref.3, ECO:0007744|PDB:2HPV |
Chain | Residue | Details |
A | HIS10 | |
D | HIS10 | |
D | SER148 | |
D | ASP184 | |
A | SER148 | |
A | ASP184 | |
B | HIS10 | |
B | SER148 | |
B | ASP184 | |
C | HIS10 | |
C | SER148 | |
C | ASP184 |
site_id | SWS_FT_FI2 |
Number of Residues | 8 |
Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_01216, ECO:0000269|Ref.3, ECO:0007744|PDB:2HPV |
Chain | Residue | Details |
A | SER17 | |
A | MSE104 | |
B | SER17 | |
B | MSE104 | |
C | SER17 | |
C | MSE104 | |
D | SER17 | |
D | MSE104 |