1F6M
CRYSTAL STRUCTURE OF A COMPLEX BETWEEN THIOREDOXIN REDUCTASE, THIOREDOXIN, AND THE NADP+ ANALOG, AADP+
Functional Information from GO Data
Chain | GOid | namespace | contents |
A | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
A | 0005515 | molecular_function | protein binding |
A | 0005737 | cellular_component | cytoplasm |
A | 0005829 | cellular_component | cytosol |
A | 0016491 | molecular_function | oxidoreductase activity |
A | 0019430 | biological_process | removal of superoxide radicals |
A | 0045454 | biological_process | cell redox homeostasis |
A | 0050660 | molecular_function | flavin adenine dinucleotide binding |
A | 1902515 | cellular_component | thioredoxin-disulfide reductase complex |
B | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
B | 0005515 | molecular_function | protein binding |
B | 0005737 | cellular_component | cytoplasm |
B | 0005829 | cellular_component | cytosol |
B | 0016491 | molecular_function | oxidoreductase activity |
B | 0019430 | biological_process | removal of superoxide radicals |
B | 0045454 | biological_process | cell redox homeostasis |
B | 0050660 | molecular_function | flavin adenine dinucleotide binding |
B | 1902515 | cellular_component | thioredoxin-disulfide reductase complex |
C | 0005515 | molecular_function | protein binding |
C | 0005737 | cellular_component | cytoplasm |
C | 0005829 | cellular_component | cytosol |
C | 0015035 | molecular_function | protein-disulfide reductase activity |
C | 0015036 | molecular_function | disulfide oxidoreductase activity |
C | 0030337 | molecular_function | DNA polymerase processivity factor activity |
C | 0045454 | biological_process | cell redox homeostasis |
D | 0005515 | molecular_function | protein binding |
D | 0005737 | cellular_component | cytoplasm |
D | 0005829 | cellular_component | cytosol |
D | 0015035 | molecular_function | protein-disulfide reductase activity |
D | 0015036 | molecular_function | disulfide oxidoreductase activity |
D | 0030337 | molecular_function | DNA polymerase processivity factor activity |
D | 0045454 | biological_process | cell redox homeostasis |
E | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
E | 0005515 | molecular_function | protein binding |
E | 0005737 | cellular_component | cytoplasm |
E | 0005829 | cellular_component | cytosol |
E | 0016491 | molecular_function | oxidoreductase activity |
E | 0019430 | biological_process | removal of superoxide radicals |
E | 0045454 | biological_process | cell redox homeostasis |
E | 0050660 | molecular_function | flavin adenine dinucleotide binding |
E | 1902515 | cellular_component | thioredoxin-disulfide reductase complex |
F | 0004791 | molecular_function | thioredoxin-disulfide reductase (NADPH) activity |
F | 0005515 | molecular_function | protein binding |
F | 0005737 | cellular_component | cytoplasm |
F | 0005829 | cellular_component | cytosol |
F | 0016491 | molecular_function | oxidoreductase activity |
F | 0019430 | biological_process | removal of superoxide radicals |
F | 0045454 | biological_process | cell redox homeostasis |
F | 0050660 | molecular_function | flavin adenine dinucleotide binding |
F | 1902515 | cellular_component | thioredoxin-disulfide reductase complex |
G | 0005515 | molecular_function | protein binding |
G | 0005737 | cellular_component | cytoplasm |
G | 0005829 | cellular_component | cytosol |
G | 0015035 | molecular_function | protein-disulfide reductase activity |
G | 0015036 | molecular_function | disulfide oxidoreductase activity |
G | 0030337 | molecular_function | DNA polymerase processivity factor activity |
G | 0045454 | biological_process | cell redox homeostasis |
H | 0005515 | molecular_function | protein binding |
H | 0005737 | cellular_component | cytoplasm |
H | 0005829 | cellular_component | cytosol |
H | 0015035 | molecular_function | protein-disulfide reductase activity |
H | 0015036 | molecular_function | disulfide oxidoreductase activity |
H | 0030337 | molecular_function | DNA polymerase processivity factor activity |
H | 0045454 | biological_process | cell redox homeostasis |
Functional Information from PDB Data
site_id | AC1 |
Number of Residues | 35 |
Details | BINDING SITE FOR RESIDUE FAD A 1500 |
Chain | Residue |
A | GLY12 |
A | GLY41 |
A | GLN42 |
A | LEU43 |
A | THR46 |
A | VAL49 |
A | ASN51 |
A | HIS83 |
A | ILE84 |
A | ALA111 |
A | THR112 |
A | SER13 |
A | GLY113 |
A | ALA114 |
A | HIS245 |
A | ILE251 |
A | GLY285 |
A | ASP286 |
A | ARG293 |
A | GLN294 |
A | ALA295 |
A | SER298 |
A | GLY14 |
A | 3AA1501 |
A | HOH1502 |
A | HOH1521 |
A | HOH1530 |
A | HOH1556 |
B | TYR23 |
A | PRO15 |
A | ALA16 |
A | THR35 |
A | GLY36 |
A | MET37 |
A | GLU38 |
site_id | AC2 |
Number of Residues | 18 |
Details | BINDING SITE FOR RESIDUE 3AA A 1501 |
Chain | Residue |
A | LEU119 |
A | GLY153 |
A | GLY154 |
A | ASN155 |
A | THR156 |
A | GLU159 |
A | HIS175 |
A | ARG176 |
A | ARG177 |
A | ARG181 |
A | ALA242 |
A | ILE243 |
A | GLY244 |
A | HIS245 |
A | TYR292 |
A | ARG293 |
A | GLN294 |
A | FAD1500 |
site_id | AC3 |
Number of Residues | 36 |
Details | BINDING SITE FOR RESIDUE FAD B 2500 |
Chain | Residue |
A | TYR23 |
B | GLY12 |
B | SER13 |
B | GLY14 |
B | PRO15 |
B | ALA16 |
B | THR35 |
B | GLY36 |
B | MET37 |
B | GLU38 |
B | GLY41 |
B | GLN42 |
B | LEU43 |
B | THR46 |
B | VAL49 |
B | ASN51 |
B | HIS83 |
B | ILE84 |
B | ALA111 |
B | THR112 |
B | GLY113 |
B | ALA114 |
B | HIS245 |
B | ASN248 |
B | ILE251 |
B | GLY285 |
B | ASP286 |
B | ARG293 |
B | GLN294 |
B | ALA295 |
B | SER298 |
B | 3AA2501 |
B | HOH2503 |
B | HOH2504 |
B | HOH2507 |
B | HOH2541 |
site_id | AC4 |
Number of Residues | 21 |
Details | BINDING SITE FOR RESIDUE 3AA B 2501 |
Chain | Residue |
B | ILE243 |
B | GLY244 |
B | HIS245 |
B | TYR292 |
B | ARG293 |
B | GLN294 |
B | FAD2500 |
B | HOH2518 |
B | HOH2529 |
B | HOH2542 |
B | HOH2557 |
B | ARG117 |
B | GLY153 |
B | GLY154 |
B | ASN155 |
B | THR156 |
B | GLU159 |
B | HIS175 |
B | ARG176 |
B | ARG177 |
B | ARG181 |
site_id | AC5 |
Number of Residues | 33 |
Details | BINDING SITE FOR RESIDUE FAD E 3500 |
Chain | Residue |
E | GLY12 |
E | SER13 |
E | GLY14 |
E | PRO15 |
E | ALA16 |
E | THR35 |
E | GLY36 |
E | MET37 |
E | GLU38 |
E | GLY41 |
E | GLN42 |
E | LEU43 |
E | THR46 |
E | VAL49 |
E | ASN51 |
E | HIS83 |
E | ILE84 |
E | ALA111 |
E | THR112 |
E | GLY113 |
E | ALA114 |
E | HIS245 |
E | ILE251 |
E | GLY285 |
E | ASP286 |
E | ARG293 |
E | GLN294 |
E | ALA295 |
E | SER298 |
E | 3AA3501 |
E | HOH3522 |
E | HOH3533 |
F | TYR23 |
site_id | AC6 |
Number of Residues | 19 |
Details | BINDING SITE FOR RESIDUE 3AA E 3501 |
Chain | Residue |
E | LEU119 |
E | GLY153 |
E | GLY154 |
E | ASN155 |
E | THR156 |
E | GLU159 |
E | HIS175 |
E | ARG176 |
E | ARG177 |
E | ARG181 |
E | ALA242 |
E | ILE243 |
E | GLY244 |
E | HIS245 |
E | TYR292 |
E | ARG293 |
E | GLN294 |
E | FAD3500 |
E | HOH3504 |
site_id | AC7 |
Number of Residues | 37 |
Details | BINDING SITE FOR RESIDUE FAD F 4500 |
Chain | Residue |
E | TYR23 |
F | GLY12 |
F | SER13 |
F | GLY14 |
F | PRO15 |
F | ALA16 |
F | THR35 |
F | GLY36 |
F | MET37 |
F | GLU38 |
F | GLY41 |
F | GLN42 |
F | LEU43 |
F | THR46 |
F | VAL49 |
F | ASN51 |
F | HIS83 |
F | ILE84 |
F | ALA111 |
F | THR112 |
F | GLY113 |
F | ALA114 |
F | HIS245 |
F | ASN248 |
F | ILE251 |
F | GLY285 |
F | ASP286 |
F | ARG293 |
F | GLN294 |
F | ALA295 |
F | SER298 |
F | 3AA4501 |
F | HOH4502 |
F | HOH4503 |
F | HOH4504 |
F | HOH4508 |
F | HOH4514 |
site_id | AC8 |
Number of Residues | 20 |
Details | BINDING SITE FOR RESIDUE 3AA F 4501 |
Chain | Residue |
F | ARG117 |
F | GLY153 |
F | GLY154 |
F | ASN155 |
F | THR156 |
F | GLU159 |
F | HIS175 |
F | ARG176 |
F | ARG177 |
F | ARG181 |
F | ILE243 |
F | GLY244 |
F | HIS245 |
F | TYR292 |
F | ARG293 |
F | GLN294 |
F | FAD4500 |
F | HOH4543 |
F | HOH4544 |
F | HOH4563 |
Functional Information from SwissProt/UniProt
site_id | SWS_FT_FI1 |
Number of Residues | 8 |
Details | ACT_SITE: Nucleophile |
Chain | Residue | Details |
C | GLY33 | |
C | LYS36 | |
D | GLY33 | |
D | LYS36 | |
G | GLY33 | |
G | LYS36 | |
H | GLY33 | |
H | LYS36 |
site_id | SWS_FT_FI2 |
Number of Residues | 4 |
Details | SITE: Deprotonates C-terminal active site Cys |
Chain | Residue | Details |
C | PHE27 | |
D | PHE27 | |
G | PHE27 | |
H | PHE27 |
site_id | SWS_FT_FI3 |
Number of Residues | 8 |
Details | SITE: Contributes to redox potential value |
Chain | Residue | Details |
C | PRO34 | |
C | SER35 | |
D | PRO34 | |
D | SER35 | |
G | PRO34 | |
G | SER35 | |
H | PRO34 | |
H | SER35 |
site_id | SWS_FT_FI4 |
Number of Residues | 4 |
Details | MOD_RES: N6-acetyllysine => ECO:0000269|PubMed:18723842 |
Chain | Residue | Details |
C | TYR70 | |
D | TYR70 | |
G | TYR70 | |
H | TYR70 |
Catalytic Information from CSA
site_id | CSA1 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1tde |
Chain | Residue | Details |
A | SER135 | |
A | CYS138 | |
A | ASP139 |
site_id | CSA2 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1tde |
Chain | Residue | Details |
B | SER135 | |
B | CYS138 | |
B | ASP139 |
site_id | CSA3 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1tde |
Chain | Residue | Details |
E | SER135 | |
E | CYS138 | |
E | ASP139 |
site_id | CSA4 |
Number of Residues | 3 |
Details | Annotated By Reference To The Literature 1tde |
Chain | Residue | Details |
F | SER135 | |
F | CYS138 | |
F | ASP139 |
site_id | CSA5 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1tde |
Chain | Residue | Details |
C | SER35 | |
C | CYS32 |
site_id | CSA6 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1tde |
Chain | Residue | Details |
D | SER35 | |
D | CYS32 |
site_id | CSA7 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1tde |
Chain | Residue | Details |
G | SER35 | |
G | CYS32 |
site_id | CSA8 |
Number of Residues | 2 |
Details | Annotated By Reference To The Literature 1tde |
Chain | Residue | Details |
H | SER35 | |
H | CYS32 |
site_id | MCSA1 |
Number of Residues | 3 |
Details | M-CSA 381 |
Chain | Residue | Details |
A | ALA136 | covalent catalysis, proton shuttle (general acid/base) |
A | ASP139 | covalent catalysis, proton shuttle (general acid/base) |
A | GLY140 | proton shuttle (general acid/base) |
site_id | MCSA2 |
Number of Residues | 3 |
Details | M-CSA 381 |
Chain | Residue | Details |
B | ALA136 | covalent catalysis, proton shuttle (general acid/base) |
B | ASP139 | covalent catalysis, proton shuttle (general acid/base) |
B | GLY140 | proton shuttle (general acid/base) |
site_id | MCSA3 |
Number of Residues | 3 |
Details | M-CSA 381 |
Chain | Residue | Details |
E | ALA136 | covalent catalysis, proton shuttle (general acid/base) |
E | ASP139 | covalent catalysis, proton shuttle (general acid/base) |
E | GLY140 | proton shuttle (general acid/base) |
site_id | MCSA4 |
Number of Residues | 3 |
Details | M-CSA 381 |
Chain | Residue | Details |
F | ALA136 | covalent catalysis, proton shuttle (general acid/base) |
F | ASP139 | covalent catalysis, proton shuttle (general acid/base) |
F | GLY140 | proton shuttle (general acid/base) |