2Z9D
The crystal structure of AzoR (azoreductase) from Escherichia coli: Oxidized AzoR in orthorhombic crystals
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0005829 | cellular_component | cytosol |
| A | 0006979 | biological_process | response to oxidative stress |
| 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 |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0050446 | molecular_function | azobenzene reductase activity |
| B | 0005829 | cellular_component | cytosol |
| B | 0006979 | biological_process | response to oxidative stress |
| 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 |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0050446 | molecular_function | azobenzene reductase activity |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FMN A 401 |
| Chain | Residue |
| A | SER9 |
| A | ASN97 |
| A | PHE98 |
| A | SER139 |
| A | ARG140 |
| A | GLY141 |
| A | GLY142 |
| A | HIS144 |
| A | HOH457 |
| B | LEU50 |
| B | ARG59 |
| A | LEU11 |
| A | SER15 |
| A | GLN16 |
| A | SER17 |
| A | ASP62 |
| A | PRO94 |
| A | MET95 |
| A | TYR96 |
| site_id | AC2 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FMN B 402 |
| Chain | Residue |
| A | LEU50 |
| A | ARG59 |
| B | SER9 |
| B | LEU11 |
| B | SER15 |
| B | GLN16 |
| B | SER17 |
| B | ASP62 |
| B | PRO94 |
| B | MET95 |
| B | TYR96 |
| B | ASN97 |
| B | PHE98 |
| B | SER139 |
| B | ARG140 |
| B | GLY141 |
| B | GLY142 |
| B | HIS144 |
| B | HOH436 |
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|PubMed:16684776, ECO:0000269|PubMed:18337254, ECO:0007744|PDB:1V4B, ECO:0007744|PDB:2D5I, ECO:0007744|PDB:2Z98, ECO:0007744|PDB:2Z9B, ECO:0007744|PDB:2Z9C, ECO:0007744|PDB:2Z9D |
| Chain | Residue | Details |
| A | SER9 | |
| A | SER15 | |
| A | MET95 | |
| B | SER9 | |
| B | SER15 | |
| B | MET95 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16684776, ECO:0000269|PubMed:18337254, ECO:0007744|PDB:1V4B, ECO:0007744|PDB:2D5I, ECO:0007744|PDB:2Z98, ECO:0007744|PDB:2Z9B, ECO:0007744|PDB:2Z9C, ECO:0007744|PDB:2Z9D |
| Chain | Residue | Details |
| A | SER139 | |
| B | SER139 |
