2CFY
Crystal structure of human thioredoxin reductase 1
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| 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 |
| B | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| B | 0016491 | molecular_function | oxidoreductase activity |
| B | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| B | 0045454 | biological_process | cell redox homeostasis |
| B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| C | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| C | 0016491 | molecular_function | oxidoreductase activity |
| C | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| C | 0045454 | biological_process | cell redox homeostasis |
| C | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| D | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| D | 0016491 | molecular_function | oxidoreductase activity |
| D | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| D | 0045454 | biological_process | cell redox homeostasis |
| D | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| E | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| E | 0016491 | molecular_function | oxidoreductase activity |
| E | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| E | 0045454 | biological_process | cell redox homeostasis |
| E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
| F | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
| F | 0016491 | molecular_function | oxidoreductase activity |
| F | 0016668 | molecular_function | oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor |
| F | 0045454 | biological_process | cell redox homeostasis |
| F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 33 |
| Details | BINDING SITE FOR RESIDUE FAD A 600 |
| Chain | Residue |
| A | ILE18 |
| A | VAL44 |
| A | GLY57 |
| A | THR58 |
| A | CYS59 |
| A | GLY63 |
| A | CYS64 |
| A | LYS67 |
| A | ALA130 |
| A | TYR131 |
| A | GLY132 |
| A | GLY19 |
| A | ALA160 |
| A | THR161 |
| A | GLY162 |
| A | TYR200 |
| A | VAL201 |
| A | ARG293 |
| A | ILE300 |
| A | GLY333 |
| A | ASP334 |
| A | GLU341 |
| A | GLY20 |
| A | LEU342 |
| A | THR343 |
| A | PRO344 |
| B | HIS472 |
| A | GLY21 |
| A | SER22 |
| A | GLY23 |
| A | LEU41 |
| A | ASP42 |
| A | PHE43 |
| site_id | AC2 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD B 600 |
| Chain | Residue |
| A | HIS472 |
| B | ILE18 |
| B | GLY19 |
| B | GLY20 |
| B | GLY21 |
| B | GLY23 |
| B | LEU41 |
| B | ASP42 |
| B | PHE43 |
| B | VAL44 |
| B | GLY57 |
| B | THR58 |
| B | CYS59 |
| B | CYS64 |
| B | LYS67 |
| B | TYR131 |
| B | GLY132 |
| B | ALA160 |
| B | THR161 |
| B | GLY162 |
| B | VAL201 |
| B | ARG293 |
| B | ILE300 |
| B | GLY333 |
| B | ASP334 |
| B | GLU341 |
| B | LEU342 |
| B | THR343 |
| B | PRO344 |
| B | HOH2003 |
| B | HOH2053 |
| site_id | AC3 |
| Number of Residues | 31 |
| Details | BINDING SITE FOR RESIDUE FAD C 600 |
| Chain | Residue |
| C | ILE18 |
| C | GLY19 |
| C | GLY20 |
| C | GLY21 |
| C | SER22 |
| C | GLY23 |
| C | LEU41 |
| C | ASP42 |
| C | PHE43 |
| C | VAL44 |
| C | GLY57 |
| C | THR58 |
| C | CYS64 |
| C | LYS67 |
| C | ALA130 |
| C | TYR131 |
| C | GLY132 |
| C | ALA160 |
| C | THR161 |
| C | GLY162 |
| C | VAL201 |
| C | ARG293 |
| C | ILE300 |
| C | GLY333 |
| C | ASP334 |
| C | GLU341 |
| C | LEU342 |
| C | THR343 |
| C | PRO344 |
| C | HOH2057 |
| D | HIS472 |
| site_id | AC4 |
| Number of Residues | 30 |
| Details | BINDING SITE FOR RESIDUE FAD D 600 |
| Chain | Residue |
| D | GLY23 |
| D | LEU41 |
| D | ASP42 |
| D | PHE43 |
| D | VAL44 |
| D | GLY57 |
| D | THR58 |
| D | CYS59 |
| D | GLY63 |
| D | CYS64 |
| D | LYS67 |
| D | ALA130 |
| D | TYR131 |
| D | GLY132 |
| D | ALA160 |
| D | THR161 |
| D | GLY162 |
| D | VAL201 |
| D | ARG293 |
| D | ILE300 |
| D | GLY333 |
| D | ASP334 |
| D | GLU341 |
| D | LEU342 |
| D | THR343 |
| D | PRO344 |
| C | HIS472 |
| D | GLY19 |
| D | GLY21 |
| D | SER22 |
| site_id | AC5 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE FAD E 600 |
| Chain | Residue |
| E | ILE18 |
| E | GLY19 |
| E | GLY21 |
| E | SER22 |
| E | GLY23 |
| E | LEU41 |
| E | ASP42 |
| E | PHE43 |
| E | VAL44 |
| E | GLY57 |
| E | THR58 |
| E | CYS59 |
| E | CYS64 |
| E | TYR131 |
| E | GLY132 |
| E | THR161 |
| E | GLY162 |
| E | ILE300 |
| E | GLY333 |
| E | ASP334 |
| E | GLU341 |
| E | LEU342 |
| E | THR343 |
| site_id | AC6 |
| Number of Residues | 19 |
| Details | BINDING SITE FOR RESIDUE FAD F 600 |
| Chain | Residue |
| F | GLY19 |
| F | GLY20 |
| F | GLY21 |
| F | GLY23 |
| F | LEU41 |
| F | ASP42 |
| F | PHE43 |
| F | VAL44 |
| F | GLY57 |
| F | THR58 |
| F | ALA130 |
| F | TYR131 |
| F | GLY132 |
| F | THR161 |
| F | GLY162 |
| F | ILE300 |
| F | GLY333 |
| F | ASP334 |
| F | ALA346 |
Functional Information from PROSITE/UniProt
| site_id | PS00076 |
| Number of Residues | 11 |
| Details | PYRIDINE_REDOX_1 Pyridine nucleotide-disulphide oxidoreductases class-I active site. GGtCVnvGCIP |
| Chain | Residue | Details |
| A | GLY56-PRO66 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 6 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS472 | |
| B | HIS472 | |
| C | HIS472 | |
| D | HIS472 | |
| E | HIS472 | |
| F | HIS472 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 72 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17512005, ECO:0007744|PDB:2J3N |
| Chain | Residue | Details |
| A | GLY172 | |
| A | LEU465 | |
| A | VAL484 | |
| A | HIS472 | |
| B | GLY172 | |
| B | LYS192 | |
| B | PHE208 | |
| B | GLY213 | |
| B | GLU281 | |
| B | ILE316 | |
| B | GLN348 | |
| A | LYS192 | |
| B | PRO371 | |
| B | GLY442 | |
| B | LEU465 | |
| B | VAL484 | |
| B | HIS472 | |
| C | GLY172 | |
| C | LYS192 | |
| C | PHE208 | |
| C | GLY213 | |
| C | GLU281 | |
| A | PHE208 | |
| C | ILE316 | |
| C | GLN348 | |
| C | PRO371 | |
| C | GLY442 | |
| C | LEU465 | |
| C | VAL484 | |
| C | HIS472 | |
| D | GLY172 | |
| D | LYS192 | |
| D | PHE208 | |
| A | GLY213 | |
| D | GLY213 | |
| D | GLU281 | |
| D | ILE316 | |
| D | GLN348 | |
| D | PRO371 | |
| D | GLY442 | |
| D | LEU465 | |
| D | VAL484 | |
| D | HIS472 | |
| E | GLY172 | |
| A | GLU281 | |
| E | LYS192 | |
| E | PHE208 | |
| E | GLY213 | |
| E | GLU281 | |
| E | ILE316 | |
| E | GLN348 | |
| E | PRO371 | |
| E | GLY442 | |
| E | LEU465 | |
| E | VAL484 | |
| A | ILE316 | |
| E | HIS472 | |
| F | GLY172 | |
| F | LYS192 | |
| F | PHE208 | |
| F | GLY213 | |
| F | GLU281 | |
| F | ILE316 | |
| F | GLN348 | |
| F | PRO371 | |
| F | GLY442 | |
| A | GLN348 | |
| F | LEU465 | |
| F | VAL484 | |
| F | HIS472 | |
| A | PRO371 | |
| A | GLY442 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | BINDING: BINDING => ECO:0007744|PDB:2J3N |
| Chain | Residue | Details |
| A | GLU311 | |
| E | SER491 | |
| F | GLU311 | |
| F | SER491 | |
| A | SER491 | |
| B | GLU311 | |
| B | SER491 | |
| C | GLU311 | |
| C | SER491 | |
| D | GLU311 | |
| D | SER491 | |
| E | GLU311 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0007744|PDB:2ZZ0, ECO:0007744|PDB:2ZZB, ECO:0007744|PDB:3QFA |
| Chain | Residue | Details |
| A | GLY350 | |
| B | GLY350 | |
| C | GLY350 | |
| D | GLY350 | |
| E | GLY350 | |
| F | GLY350 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 6 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O89049 |
| Chain | Residue | Details |
| A | THR376 | |
| B | THR376 | |
| C | THR376 | |
| D | THR376 | |
| E | THR376 | |
| F | THR376 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 6 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9JMH6 |
| Chain | Residue | Details |
| A | VAL218 | |
| B | VAL218 | |
| C | VAL218 | |
| D | VAL218 | |
| E | VAL218 | |
| F | VAL218 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 6 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455 |
| Chain | Residue | Details |
| A | GLU281 | |
| B | GLU281 | |
| C | GLU281 | |
| D | GLU281 | |
| E | GLU281 | |
| F | GLU281 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 12 |
| Details | CROSSLNK: Cysteinyl-selenocysteine (Cys-Sec) => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS497 | |
| E | GLY498 | |
| F | CYS497 | |
| F | GLY498 | |
| A | GLY498 | |
| B | CYS497 | |
| B | GLY498 | |
| C | CYS497 | |
| C | GLY498 | |
| D | CYS497 | |
| D | GLY498 | |
| E | CYS497 |
