1GRF
SUBSTRATE BINDING AND CATALYSIS BY GLUTATHIONE REDUCTASE AS DERIVED FROM REFINED ENZYME: SUBSTRATE CRYSTAL STRUCTURES AT 2 ANGSTROMS RESOLUTION
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004362 | molecular_function | glutathione-disulfide reductase (NADPH) activity |
| A | 0005737 | cellular_component | cytoplasm |
| A | 0005739 | cellular_component | mitochondrion |
| A | 0005759 | cellular_component | mitochondrial matrix |
| A | 0005829 | cellular_component | cytosol |
| A | 0006749 | biological_process | glutathione metabolic process |
| A | 0009055 | molecular_function | electron transfer activity |
| A | 0009897 | cellular_component | external side of plasma membrane |
| A | 0016491 | molecular_function | oxidoreductase activity |
| A | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| A | 0034599 | biological_process | cellular response to oxidative stress |
| A | 0045454 | biological_process | cell redox homeostasis |
| A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| A | 0050661 | molecular_function | NADP binding |
| A | 0070062 | cellular_component | extracellular exosome |
| A | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE PO4 A 480 |
| Chain | Residue |
| A | HIS219 |
| A | ARG224 |
| A | HOH500 |
| A | HOH570 |
| A | HOH595 |
| A | HOH729 |
| site_id | AC2 |
| Number of Residues | 37 |
| Details | BINDING SITE FOR RESIDUE FAD A 479 |
| Chain | Residue |
| A | GLY31 |
| A | GLU50 |
| A | SER51 |
| A | HIS52 |
| A | GLY56 |
| A | THR57 |
| A | CYS58 |
| A | VAL61 |
| A | GLY62 |
| A | CYS63 |
| A | LYS66 |
| A | GLY128 |
| A | HIS129 |
| A | ALA130 |
| A | ALA155 |
| A | THR156 |
| A | GLY157 |
| A | TYR197 |
| A | ARG291 |
| A | GLY330 |
| A | ASP331 |
| A | LEU337 |
| A | LEU338 |
| A | THR339 |
| A | PRO340 |
| A | HIS467 |
| A | PRO468 |
| A | HOH483 |
| A | HOH485 |
| A | HOH496 |
| A | HOH535 |
| A | HOH803 |
| A | HOH840 |
| A | HOH999 |
| A | GLY27 |
| A | GLY29 |
| A | SER30 |
| site_id | AC3 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE ACM A 481 |
| Chain | Residue |
| A | CYS58 |
| A | VAL59 |
| A | VAL64 |
| A | TYR114 |
| A | HIS467 |
Functional Information from PROSITE/UniProt
| site_id | PS00076 |
| Number of Residues | 11 |
| Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCVP |
| Chain | Residue | Details |
| A | GLY55-PRO65 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | PHE94 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P47791 |
| Chain | Residue | Details |
| A | ARG97 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | HIS467 | |
| A | GLU472 |
| site_id | CSA2 |
| Number of Residues | 5 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | CYS58 | |
| A | GLU201 | |
| A | TYR197 | |
| A | LYS66 | |
| A | CYS63 |
| site_id | MCSA1 |
| Number of Residues | 5 |
| Details | M-CSA 6 |
| Chain | Residue | Details |
| A | LYS102 | electrofuge, electrophile, nucleofuge, nucleophile |
| A | VAL107 | electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | LEU110 | activator, electrostatic stabiliser, hydrogen bond donor |
| A | ALA241 | activator |
| A | VAL245 | activator, electrostatic stabiliser, hydrogen bond acceptor |
