2AAQ
Crystal Structure Analysis of the human Glutahione Reductase, complexed with GoPI
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 | 4 |
| Details | BINDING SITE FOR RESIDUE PO4 A 501 |
| Chain | Residue |
| A | ARG218 |
| A | HIS219 |
| A | HOH883 |
| A | HOH931 |
| site_id | AC2 |
| Number of Residues | 7 |
| Details | BINDING SITE FOR RESIDUE PO4 A 503 |
| Chain | Residue |
| A | HOH839 |
| A | HOH877 |
| A | ALA195 |
| A | ARG218 |
| A | HIS219 |
| A | ARG224 |
| A | HOH835 |
| site_id | AC3 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 504 |
| Chain | Residue |
| A | CYS58 |
| A | VAL59 |
| A | CYS63 |
| A | VAL64 |
| A | HIS467 |
| A | AU603 |
| A | K701 |
| A | GOL806 |
| site_id | AC4 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE PO4 A 502 |
| Chain | Residue |
| A | HIS75 |
| A | SER76 |
| A | MET79 |
| A | MET79 |
| A | ASP81 |
| A | HIS82 |
| A | TYR85 |
| A | PHE87 |
| site_id | AC5 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 700 |
| Chain | Residue |
| A | LYS53 |
| A | LEU54 |
| A | HOH946 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE K A 701 |
| Chain | Residue |
| A | CYS58 |
| A | PO4504 |
| A | GOL806 |
| site_id | AC7 |
| Number of Residues | 35 |
| Details | BINDING SITE FOR RESIDUE FAD A 499 |
| Chain | Residue |
| A | GLY27 |
| A | GLY29 |
| A | SER30 |
| A | GLY31 |
| A | VAL49 |
| A | GLU50 |
| A | SER51 |
| A | LYS53 |
| A | GLY56 |
| A | THR57 |
| A | CYS58 |
| A | VAL61 |
| A | CYS63 |
| A | LYS66 |
| A | HIS129 |
| A | ALA130 |
| A | ALA155 |
| A | THR156 |
| A | GLY157 |
| A | SER177 |
| A | PHE181 |
| A | ARG291 |
| A | ASP331 |
| A | LEU337 |
| A | LEU338 |
| A | THR339 |
| A | PRO340 |
| A | HIS467 |
| A | PRO468 |
| A | AU603 |
| A | HOH812 |
| A | HOH814 |
| A | HOH819 |
| A | HOH834 |
| A | HOH848 |
| site_id | AC8 |
| Number of Residues | 8 |
| Details | BINDING SITE FOR RESIDUE AUP A 601 |
| Chain | Residue |
| A | LEU173 |
| A | ILE175 |
| A | GLY179 |
| A | GLN182 |
| A | LEU261 |
| A | ASP283 |
| A | CYS284 |
| A | AU602 |
| site_id | AC9 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE AU A 602 |
| Chain | Residue |
| A | CYS284 |
| A | AUP601 |
| site_id | BC1 |
| Number of Residues | 5 |
| Details | BINDING SITE FOR RESIDUE AU A 603 |
| Chain | Residue |
| A | CYS58 |
| A | CYS63 |
| A | THR339 |
| A | FAD499 |
| A | PO4504 |
| site_id | BC2 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 804 |
| Chain | Residue |
| A | GLY196 |
| A | TYR197 |
| A | ILE198 |
| A | HOH877 |
| A | HOH878 |
| A | HOH945 |
| site_id | BC3 |
| Number of Residues | 6 |
| Details | BINDING SITE FOR RESIDUE GOL A 805 |
| Chain | Residue |
| A | GLN319 |
| A | GLY330 |
| A | CYS333 |
| A | GLY334 |
| A | LYS335 |
| A | TYR364 |
| site_id | BC4 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE GOL A 806 |
| Chain | Residue |
| A | HIS467 |
| A | PO4504 |
| A | K701 |
| A | HOH926 |
| site_id | BC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE GOL A 807 |
| Chain | Residue |
| A | ARG347 |
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 | ACT_SITE: Proton acceptor |
| Chain | Residue | Details |
| A | HIS467 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 1 |
| Details | BINDING: |
| Chain | Residue | Details |
| A | GLU50 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | MOD_RES: N6-acetyllysine => ECO:0000250|UniProtKB:P47791 |
| Chain | Residue | Details |
| A | LYS53 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | CYS58 | |
| A | CYS63 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | HIS467 | |
| A | GLU472 |
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 6 |
| Chain | Residue | Details |
| A | CYS58 | electrofuge, electrophile, nucleofuge, nucleophile |
| A | CYS63 | electrofuge, electrophile, hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | LYS66 | activator, electrostatic stabiliser, hydrogen bond donor |
| A | TYR197 | activator |
| A | GLU201 | activator, electrostatic stabiliser, hydrogen bond acceptor |
| A | HIS467 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| A | GLU472 | activator, electrostatic stabiliser, hydrogen bond acceptor |
