2ZZC
Crystal structure of NADP(H):human thioredoxin reductase I
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 | 31 |
Details | BINDING SITE FOR RESIDUE FAD A 900 |
Chain | Residue |
A | ILE18 |
A | THR58 |
A | CYS59 |
A | VAL62 |
A | GLY63 |
A | CYS64 |
A | LYS67 |
A | ALA130 |
A | TYR131 |
A | GLY132 |
A | ALA160 |
A | GLY19 |
A | THR161 |
A | GLY162 |
A | ARG293 |
A | GLY333 |
A | ASP334 |
A | GLU341 |
A | LEU342 |
A | THR343 |
A | PRO344 |
A | HOH631 |
A | GLY21 |
A | NAP901 |
B | HIS472 |
A | SER22 |
A | GLY23 |
A | LEU41 |
A | ASP42 |
A | PHE43 |
A | GLY57 |
site_id | AC2 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE NAP A 901 |
Chain | Residue |
A | LYS67 |
A | LEU168 |
A | ALA198 |
A | SER199 |
A | TYR200 |
A | VAL201 |
A | GLU204 |
A | ARG221 |
A | SER222 |
A | ARG226 |
A | VAL252 |
A | ALA290 |
A | ILE291 |
A | GLY292 |
A | GLU341 |
A | LEU342 |
A | THR373 |
A | HOH541 |
A | HOH563 |
A | HOH690 |
A | FAD900 |
site_id | AC3 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE FAD B 900 |
Chain | Residue |
A | HIS472 |
A | PRO473 |
B | GLY19 |
B | GLY21 |
B | SER22 |
B | GLY23 |
B | ASP42 |
B | PHE43 |
B | GLY57 |
B | THR58 |
B | CYS59 |
B | VAL62 |
B | GLY63 |
B | CYS64 |
B | LYS67 |
B | ALA130 |
B | TYR131 |
B | GLY132 |
B | ALA160 |
B | THR161 |
B | GLY162 |
B | ARG293 |
B | ILE300 |
B | GLY333 |
B | ASP334 |
B | GLU341 |
B | LEU342 |
B | THR343 |
B | PRO344 |
B | HOH537 |
B | HOH631 |
B | HOH727 |
B | NAP901 |
site_id | AC4 |
Number of Residues | 22 |
Details | BINDING SITE FOR RESIDUE NAP B 901 |
Chain | Residue |
B | LEU342 |
B | THR373 |
B | PHE375 |
B | HOH630 |
B | HOH736 |
B | HOH768 |
B | HOH769 |
B | FAD900 |
B | LYS67 |
B | LEU168 |
B | ALA198 |
B | SER199 |
B | TYR200 |
B | VAL201 |
B | GLU204 |
B | ARG221 |
B | SER222 |
B | ARG226 |
B | ILE291 |
B | GLY292 |
B | ARG293 |
B | GLU341 |
site_id | AC5 |
Number of Residues | 32 |
Details | BINDING SITE FOR RESIDUE FAD C 900 |
Chain | Residue |
C | ILE18 |
C | GLY19 |
C | GLY21 |
C | SER22 |
C | GLY23 |
C | ASP42 |
C | PHE43 |
C | GLY57 |
C | THR58 |
C | CYS59 |
C | VAL62 |
C | GLY63 |
C | CYS64 |
C | LYS67 |
C | ALA130 |
C | TYR131 |
C | GLY132 |
C | ALA160 |
C | THR161 |
C | GLY162 |
C | ARG293 |
C | GLY333 |
C | ASP334 |
C | GLU341 |
C | LEU342 |
C | THR343 |
C | PRO344 |
C | HOH596 |
C | NAP901 |
D | HIS472 |
D | PRO473 |
D | HOH516 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE NAP C 901 |
Chain | Residue |
C | LYS67 |
C | LEU168 |
C | ALA198 |
C | SER199 |
C | TYR200 |
C | VAL201 |
C | GLU204 |
C | ARG221 |
C | SER222 |
C | ARG226 |
C | VAL252 |
C | ILE291 |
C | GLY292 |
C | ARG293 |
C | GLU341 |
C | LEU342 |
C | THR373 |
C | HOH515 |
C | FAD900 |
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 | GLY57 |
D | THR58 |
D | CYS59 |
D | VAL62 |
D | GLY63 |
D | CYS64 |
D | LYS67 |
D | ALA130 |
D | TYR131 |
D | GLY132 |
D | ALA160 |
D | THR161 |
D | GLY162 |
D | ARG293 |
D | GLY333 |
D | ASP334 |
D | GLU341 |
D | LEU342 |
D | THR343 |
D | PRO344 |
D | HOH567 |
D | HOH891 |
D | NAP901 |
site_id | AC8 |
Number of Residues | 23 |
Details | BINDING SITE FOR RESIDUE NAP D 901 |
Chain | Residue |
D | LYS67 |
D | LEU168 |
D | GLY197 |
D | ALA198 |
D | SER199 |
D | TYR200 |
D | VAL201 |
D | GLU204 |
D | ARG221 |
D | SER222 |
D | ARG226 |
D | VAL252 |
D | ALA290 |
D | ILE291 |
D | GLY292 |
D | ARG293 |
D | GLU341 |
D | LEU342 |
D | THR373 |
D | HOH560 |
D | HOH580 |
D | HOH595 |
D | FAD900 |
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 |