2GRT
HUMAN GLUTATHIONE REDUCTASE A34E, R37W MUTANT, OXIDIZED GLUTATHIONE COMPLEX
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004362 | molecular_function | glutathione-disulfide reductase (NADPH) activity |
A | 0006749 | biological_process | glutathione metabolic process |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
A | 0045454 | biological_process | cell redox homeostasis |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 0050661 | molecular_function | NADP binding |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE FAD A 479 |
Chain | Residue |
A | LYS53 |
A | GLY56 |
A | THR57 |
A | CYS58 |
A | VAL61 |
A | GLY62 |
A | CYS63 |
A | LYS66 |
A | GLY128 |
A | HIS129 |
A | ILE26 |
A | ALA130 |
A | ALA155 |
A | THR156 |
A | GLY157 |
A | TYR197 |
A | ARG291 |
A | GLY330 |
A | ASP331 |
A | LEU337 |
A | LEU338 |
A | GLY27 |
A | THR339 |
A | PRO340 |
A | ALA342 |
A | HIS467 |
A | PRO468 |
A | GLY29 |
A | SER30 |
A | GLY31 |
A | GLU50 |
A | SER51 |
A | HIS52 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE GDS A 481 |
Chain | Residue |
A | SER30 |
A | GLU34 |
A | TRP37 |
A | VAL59 |
A | VAL64 |
A | TYR106 |
A | LEU110 |
A | ILE113 |
A | TYR114 |
A | ASN117 |
A | ILE343 |
A | PHE403 |
A | MET406 |
A | HIS467 |
A | THR469 |
A | GLU472 |
A | GLU473 |
A | THR476 |
site_id | S1 |
Number of Residues | 1 |
Details | THE ACTIVE SITE HISTIDINE (HIS 467) IS FROM THE OTHER SUBUNIT. |
Chain | Residue |
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 |