2ZZ0
Crystal structure of human thioredoxin reductase I (SeCys 498 Cys)
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 |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD A 900 |
| Chain | Residue |
| A | ILE18 |
| A | GLY57 |
| A | THR58 |
| A | CYS59 |
| A | VAL62 |
| A | GLY63 |
| A | CYS64 |
| A | LYS67 |
| A | ALA130 |
| A | TYR131 |
| A | GLY132 |
| A | GLY19 |
| A | THR161 |
| A | GLY162 |
| A | TYR200 |
| A | ARG293 |
| A | ILE300 |
| A | GLY333 |
| A | ASP334 |
| A | GLU341 |
| A | LEU342 |
| A | THR343 |
| A | GLY21 |
| A | PRO344 |
| A | HOH572 |
| B | HIS472 |
| A | SER22 |
| A | GLY23 |
| A | LEU41 |
| A | ASP42 |
| A | PHE43 |
| A | VAL44 |
| site_id | AC2 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 A 901 |
| Chain | Residue |
| A | ARG221 |
| A | SER222 |
| A | ARG226 |
| site_id | AC3 |
| Number of Residues | 34 |
| Details | BINDING SITE FOR RESIDUE FAD B 900 |
| Chain | Residue |
| A | HIS472 |
| A | PRO473 |
| B | ILE18 |
| B | GLY19 |
| B | GLY21 |
| B | SER22 |
| B | GLY23 |
| B | LEU41 |
| B | ASP42 |
| B | PHE43 |
| B | VAL44 |
| B | GLY57 |
| B | THR58 |
| B | CYS59 |
| B | VAL62 |
| B | GLY63 |
| B | CYS64 |
| B | LYS67 |
| B | ALA130 |
| B | TYR131 |
| B | GLY132 |
| B | THR161 |
| B | GLY162 |
| B | TYR200 |
| B | VAL201 |
| B | ARG293 |
| B | ILE300 |
| B | GLY333 |
| B | ASP334 |
| B | GLU341 |
| B | LEU342 |
| B | THR343 |
| B | PRO344 |
| B | HOH528 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 B 901 |
| Chain | Residue |
| B | ARG221 |
| B | SER222 |
| B | ARG226 |
| site_id | AC5 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD C 900 |
| Chain | Residue |
| C | GLU341 |
| C | LEU342 |
| C | THR343 |
| C | PRO344 |
| D | HIS472 |
| C | ILE18 |
| C | GLY19 |
| C | GLY21 |
| C | SER22 |
| C | GLY23 |
| C | LEU41 |
| C | ASP42 |
| C | PHE43 |
| C | VAL44 |
| C | GLY57 |
| C | THR58 |
| C | CYS59 |
| C | VAL62 |
| C | GLY63 |
| C | CYS64 |
| C | LYS67 |
| C | ALA130 |
| C | TYR131 |
| C | GLY132 |
| C | THR161 |
| C | GLY162 |
| C | TYR200 |
| C | VAL201 |
| C | ARG293 |
| C | ILE300 |
| C | GLY333 |
| C | ASP334 |
| site_id | AC6 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 C 901 |
| Chain | Residue |
| C | ARG221 |
| C | SER222 |
| C | ARG226 |
| site_id | AC7 |
| Number of Residues | 32 |
| Details | BINDING SITE FOR RESIDUE FAD D 900 |
| Chain | Residue |
| C | HIS472 |
| C | PRO473 |
| D | ILE18 |
| D | GLY19 |
| D | GLY21 |
| D | SER22 |
| D | GLY23 |
| D | ASP42 |
| D | PHE43 |
| D | VAL44 |
| D | GLY57 |
| D | THR58 |
| D | CYS59 |
| D | VAL62 |
| D | GLY63 |
| D | CYS64 |
| D | LYS67 |
| D | ALA130 |
| D | TYR131 |
| D | GLY132 |
| D | THR161 |
| D | GLY162 |
| D | TYR200 |
| D | VAL201 |
| D | ARG293 |
| D | GLY333 |
| D | ASP334 |
| D | GLU341 |
| D | LEU342 |
| D | THR343 |
| D | PRO344 |
| D | PHE375 |
| site_id | AC8 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE SO4 D 901 |
| Chain | Residue |
| D | ARG221 |
| D | SER222 |
| D | ARG226 |
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 | 4 |
| Details | ACT_SITE: Proton acceptor => ECO:0000250 |
| Chain | Residue | Details |
| A | HIS472 | |
| B | HIS472 | |
| C | HIS472 | |
| D | HIS472 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 48 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:17512005, ECO:0007744|PDB:2J3N |
| Chain | Residue | Details |
| A | SER22 | |
| A | LYS315 | |
| A | ASP334 | |
| A | HIS472 | |
| B | SER22 | |
| B | ASP42 | |
| B | THR58 | |
| B | GLY63 | |
| B | TYR131 | |
| B | ARG166 | |
| B | ALA198 | |
| A | ASP42 | |
| B | ARG221 | |
| B | GLY292 | |
| B | LYS315 | |
| B | ASP334 | |
| B | HIS472 | |
| C | SER22 | |
| C | ASP42 | |
| C | THR58 | |
| C | GLY63 | |
| C | TYR131 | |
| A | THR58 | |
| C | ARG166 | |
| C | ALA198 | |
| C | ARG221 | |
| C | GLY292 | |
| C | LYS315 | |
| C | ASP334 | |
| C | HIS472 | |
| D | SER22 | |
| D | ASP42 | |
| D | THR58 | |
| A | GLY63 | |
| D | GLY63 | |
| D | TYR131 | |
| D | ARG166 | |
| D | ALA198 | |
| D | ARG221 | |
| D | GLY292 | |
| D | LYS315 | |
| D | ASP334 | |
| D | HIS472 | |
| A | TYR131 | |
| A | ARG166 | |
| A | ALA198 | |
| A | ARG221 | |
| A | GLY292 |
| site_id | SWS_FT_FI3 |
| Number of Residues | 8 |
| Details | BINDING: BINDING => ECO:0007744|PDB:2J3N |
| Chain | Residue | Details |
| A | THR161 | |
| A | GLU341 | |
| B | THR161 | |
| B | GLU341 | |
| C | THR161 | |
| C | GLU341 | |
| D | THR161 | |
| D | GLU341 |
| site_id | SWS_FT_FI4 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0007744|PDB:2ZZ0, ECO:0007744|PDB:2ZZB, ECO:0007744|PDB:3QFA |
| Chain | Residue | Details |
| A | TYR200 | |
| B | TYR200 | |
| C | TYR200 | |
| D | TYR200 |
| site_id | SWS_FT_FI5 |
| Number of Residues | 4 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:O89049 |
| Chain | Residue | Details |
| A | ARG226 | |
| B | ARG226 | |
| C | ARG226 | |
| D | ARG226 |
| site_id | SWS_FT_FI6 |
| Number of Residues | 4 |
| Details | MOD_RES: N6-succinyllysine => ECO:0000250|UniProtKB:Q9JMH6 |
| Chain | Residue | Details |
| A | LYS68 | |
| B | LYS68 | |
| C | LYS68 | |
| D | LYS68 |
| site_id | SWS_FT_FI7 |
| Number of Residues | 4 |
| Details | MOD_RES: Phosphotyrosine => ECO:0007744|PubMed:15592455 |
| Chain | Residue | Details |
| A | TYR131 | |
| B | TYR131 | |
| C | TYR131 | |
| D | TYR131 |
| site_id | SWS_FT_FI8 |
| Number of Residues | 8 |
| Details | CROSSLNK: Cysteinyl-selenocysteine (Cys-Sec) => ECO:0000250 |
| Chain | Residue | Details |
| A | CYS497 | |
| A | CYS498 | |
| B | CYS497 | |
| B | CYS498 | |
| C | CYS497 | |
| C | CYS498 | |
| D | CYS497 | |
| D | CYS498 |
Catalytic Information from CSA
| site_id | CSA1 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | CYS64 | |
| A | CYS59 |
| site_id | CSA10 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | ASP181 | |
| B | CYS177 | |
| B | SER180 |
| site_id | CSA11 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| C | ASP181 | |
| C | CYS177 | |
| C | SER180 |
| site_id | CSA12 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| D | ASP181 | |
| D | CYS177 | |
| D | SER180 |
| site_id | CSA2 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | CYS64 | |
| B | CYS59 |
| site_id | CSA3 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| C | CYS64 | |
| C | CYS59 |
| site_id | CSA4 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| D | CYS64 | |
| D | CYS59 |
| site_id | CSA5 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | HIS472 | |
| A | GLU477 |
| site_id | CSA6 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| B | HIS472 | |
| B | GLU477 |
| site_id | CSA7 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| C | HIS472 | |
| C | GLU477 |
| site_id | CSA8 |
| Number of Residues | 2 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| D | HIS472 | |
| D | GLU477 |
| site_id | CSA9 |
| Number of Residues | 3 |
| Details | Annotated By Reference To The Literature 1get |
| Chain | Residue | Details |
| A | ASP181 | |
| A | CYS177 | |
| A | SER180 |
