1XAN
HUMAN GLUTATHIONE REDUCTASE IN COMPLEX WITH A XANTHENE INHIBITOR
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 | 39 |
| Details | BINDING SITE FOR RESIDUE FAD A 499 |
| Chain | Residue |
| A | GLY27 |
| A | THR57 |
| A | CYS58 |
| A | GLY62 |
| A | CYS63 |
| A | LYS66 |
| A | GLY128 |
| A | HIS129 |
| A | ALA130 |
| A | ALA155 |
| A | THR156 |
| A | GLY29 |
| A | GLY157 |
| A | TYR197 |
| A | ARG291 |
| A | LEU298 |
| A | GLY330 |
| A | ASP331 |
| A | LEU337 |
| A | LEU338 |
| A | THR339 |
| A | PRO340 |
| A | SER30 |
| A | HIS467 |
| A | PRO468 |
| A | HOH502 |
| A | HOH504 |
| A | HOH510 |
| A | HOH515 |
| A | HOH554 |
| A | HOH826 |
| A | HOH859 |
| A | HOH864 |
| A | GLY31 |
| A | VAL49 |
| A | GLU50 |
| A | SER51 |
| A | HIS52 |
| A | GLY56 |
| site_id | AC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HXP A 1024 |
| Chain | Residue |
| A | ASN71 |
| A | ASN71 |
| A | VAL74 |
| A | VAL74 |
| A | HIS75 |
| A | PHE78 |
| A | PHE78 |
| A | HIS82 |
| A | HIS82 |
| A | TYR407 |
| A | HOH561 |
| A | HOH820 |
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: BINDING => ECO:0000269|PubMed:18638483, ECO:0000269|PubMed:2585516, ECO:0000269|PubMed:9546215, ECO:0007744|PDB:1DNC, ECO:0007744|PDB:1GRE, ECO:0007744|PDB:1GSN, ECO:0007744|PDB:3DK8 |
| Chain | Residue | Details |
| A | VAL74 |
| Chain | Residue | Details |
| A | HIS75 | |
| A | PHE94 | |
| A | GLU101 | |
| A | LEU110 | |
| A | GLY174 | |
| A | PRO375 | |
| A | THR383 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18638483, ECO:0000269|PubMed:2585516, ECO:0000269|PubMed:9546215, ECO:0007744|PDB:1DNC, ECO:0007744|PDB:1GRA, ECO:0007744|PDB:1GRE, ECO:0007744|PDB:1GSN |
| Chain | Residue | Details |
| A | ASP81 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:16910673, ECO:0000269|PubMed:18638483, ECO:0000269|PubMed:2585516, ECO:0000269|PubMed:3656429, ECO:0000269|PubMed:8626496, ECO:0000269|PubMed:9174360, ECO:0000269|PubMed:9546215, ECO:0007744|PDB:1BWC, ECO:0007744|PDB:1GRA, ECO:0007744|PDB:1GRG, ECO:0007744|PDB:1GRT, ECO:0007744|PDB:1K4Q, ECO:0007744|PDB:2AAQ, ECO:0007744|PDB:2GRT, ECO:0007744|PDB:3DJJ, ECO:0007744|PDB:3DK4, ECO:0007744|PDB:3DK9, ECO:0007744|PDB:3GRS, ECO:0007744|PDB:3GRT, ECO:0007744|PDB:3SQP, ECO:0007744|PDB:5GRT |
| Chain | Residue | Details |
| A | LYS102 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18638483, ECO:0000269|PubMed:2585516, ECO:0000269|PubMed:9546215, ECO:0007744|PDB:1DNC, ECO:0007744|PDB:1GRA, ECO:0007744|PDB:1GRE, ECO:0007744|PDB:1GSN, ECO:0007744|PDB:3DK4, ECO:0007744|PDB:3DK8 |
| Chain | Residue | Details |
| A | GLY158 | |
| A | TYR391 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 5 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18638483, ECO:0000269|PubMed:2585516, ECO:0007744|PDB:1GRB, ECO:0007744|PDB:3DJG, ECO:0007744|PDB:3DJJ |
| Chain | Residue | Details |
| A | GLU239 | |
| A | GLY242 | |
| A | GLU262 | |
| A | ALA268 | |
| A | GLY334 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18638483, ECO:0000269|PubMed:2585516, ECO:0007744|PDB:3DJG, ECO:0007744|PDB:3DJJ |
| Chain | Residue | Details |
| A | VAL245 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18638483, ECO:0000269|PubMed:2585516, ECO:0007744|PDB:1GRB, ECO:0007744|PDB:3DJG |
| Chain | Residue | Details |
| A | GLY381 |
| site_id | SWS_FT_FI9 |
| Number of Residues | 1 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:18638483, ECO:0000269|PubMed:2585516, ECO:0007744|PDB:3DJG |
| Chain | Residue | Details |
| A | LYS414 |
| site_id | SWS_FT_FI10 |
| 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 | 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 |
