5GXU
Cystal structure of Arabidopsis ATR2
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0003958 | molecular_function | NADPH-hemoprotein reductase activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005783 | cellular_component | endoplasmic reticulum |
| A | 0005789 | cellular_component | endoplasmic reticulum membrane |
| A | 0005886 | cellular_component | plasma membrane |
| A | 0009507 | cellular_component | chloroplast |
| A | 0009698 | biological_process | phenylpropanoid metabolic process |
| A | 0010181 | molecular_function | FMN binding |
| A | 0016020 | cellular_component | membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050661 | molecular_function | NADP binding |
| B | 0003958 | molecular_function | NADPH-hemoprotein reductase activity |
| B | 0005737 | cellular_component | cytoplasm |
| B | 0005783 | cellular_component | endoplasmic reticulum |
| B | 0005789 | cellular_component | endoplasmic reticulum membrane |
| B | 0005886 | cellular_component | plasma membrane |
| B | 0009507 | cellular_component | chloroplast |
| B | 0009698 | biological_process | phenylpropanoid metabolic process |
| B | 0010181 | molecular_function | FMN binding |
| B | 0016020 | cellular_component | membrane |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016651 | molecular_function | oxidoreductase activity, acting on NAD(P)H |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| B | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 20 |
| Details | binding site for residue FMN A 801 |
| Chain | Residue |
| A | THR111 |
| A | GLY169 |
| A | GLY171 |
| A | LEU204 |
| A | GLY205 |
| A | ASN206 |
| A | TYR209 |
| A | HIS211 |
| A | PHE212 |
| A | ASN213 |
| A | ASP239 |
| A | GLN112 |
| A | HOH986 |
| A | THR113 |
| A | GLY114 |
| A | THR115 |
| A | ALA116 |
| A | ALA166 |
| A | THR167 |
| A | TYR168 |
| site_id | AC2 |
| Number of Residues | 31 |
| Details | binding site for residue FAD A 802 |
| Chain | Residue |
| A | LEU414 |
| A | SER416 |
| A | GLN458 |
| A | ARG489 |
| A | PHE490 |
| A | TYR491 |
| A | SER492 |
| A | THR507 |
| A | CYS508 |
| A | ALA509 |
| A | VAL511 |
| A | GLU513 |
| A | MET515 |
| A | ARG519 |
| A | HIS521 |
| A | GLY523 |
| A | VAL524 |
| A | CYS525 |
| A | SER526 |
| A | THR570 |
| A | ASP709 |
| A | TRP711 |
| A | HOH921 |
| A | HOH923 |
| A | HOH944 |
| A | HOH947 |
| A | HOH957 |
| A | HOH965 |
| A | HOH981 |
| A | HOH1015 |
| A | HOH1056 |
| site_id | AC3 |
| Number of Residues | 30 |
| Details | binding site for residue FAD B 801 |
| Chain | Residue |
| B | LEU414 |
| B | SER415 |
| B | SER416 |
| B | GLN458 |
| B | ARG489 |
| B | PHE490 |
| B | TYR491 |
| B | SER492 |
| B | THR507 |
| B | CYS508 |
| B | ALA509 |
| B | VAL511 |
| B | GLU513 |
| B | MET515 |
| B | ARG519 |
| B | HIS521 |
| B | GLY523 |
| B | VAL524 |
| B | CYS525 |
| B | SER526 |
| B | THR570 |
| B | TRP711 |
| B | HOH924 |
| B | HOH925 |
| B | HOH941 |
| B | HOH951 |
| B | HOH1000 |
| B | HOH1001 |
| B | HOH1017 |
| B | HOH1022 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1276 |
| Details | TOPO_DOM: Cytoplasmic => ECO:0000255|HAMAP-Rule:MF_03212 |
| Chain | Residue | Details |
| A | ARG73-TRP711 | |
| B | ARG73-TRP711 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 26 |
| Details | BINDING: BINDING => ECO:0000255|HAMAP-Rule:MF_03212 |
| Chain | Residue | Details |
| A | THR111 | |
| A | SER631 | |
| A | LYS637 | |
| A | ASP673 | |
| A | TRP711 | |
| B | THR111 | |
| B | ALA166 | |
| B | LEU204 | |
| B | ASP239 | |
| B | ARG330 | |
| B | ARG489 | |
| A | ALA166 | |
| B | THR507 | |
| B | GLY523 | |
| B | THR570 | |
| B | SER631 | |
| B | LYS637 | |
| B | ASP673 | |
| B | TRP711 | |
| A | LEU204 | |
| A | ASP239 | |
| A | ARG330 | |
| A | ARG489 | |
| A | THR507 | |
| A | GLY523 | |
| A | THR570 |
